Human Metabolome Database Version 2.5

Showing metabocard for 5-Hydroxyindoleacetaldehyde (HMDB04073)

Legend: metabolite field enzyme field

Version

2.5

Creation Date

2006-08-13 11:19:52

Update Date

2009-05-05 20:59:59

Accession Number

HMDB04073

Secondary Accession Numbers

Not Available

Common Name

5-Hydroxyindoleacetaldehyde

Description

5-Hydroxyindoleacetaldehyde is a biogenic aldehyde of serotonin derived from the action of monoamine oxidase (MAO). (PMIDs 11306106, 2470392)

Synonyms

(5-hydroxy-1H-indol-3-yl)acetaldehyde
(5-hydroxyindol-3-yl)acetaldehyde
5-Hial
5-Hydroxyindole-3-acetaldehyde
5-hydroxy-1H-Indole-3-acetaldehyde
Hydroxyindoleacetaldehyde

Chemical IUPAC Name

2-(5-hydroxy-1H-indol-3-yl)acetaldehyde

Chemical Formula

C₁₀H₉NO₂

Chemical Structure

Chemical Taxonomy

Kingdom
Organic
Super Class
Heterocyclic molecules
Class
Indoles and Indole Derivatives
Sub Class
Miscellaneous Indoles
Family
Mammalian Metabolite
Species
aldehyde phenol or hydroxyhetarene aromatic compound heterocyclic compound
Biofunction
—
Application
—
Source
Endogenous

Average Molecular Weight

175.184

Monoisotopic Molecular Weight

175.063324

Isomeric SMILES

OC1=CC2=C(NC=C2CC=O)C=C1

Canonical SMILES

OC1=CC2=C(NC=C2CC=O)C=C1

KEGG Compound ID

C05634

BioCyc ID

Not Available

BiGG ID

46165

Wikipedia Link

Not Available

NuGOwiki Link

HMDB04073

Metagene Link

HMDB04073

METLIN ID

Not Available

PubChem Compound

74688

PubChem Substance

7945

ChEBI ID

2070

CAS Registry Number

1892-21-3

InChI Identifier

InChI=1/C10H9NO2/c12-4-3-7-6-11-10-2-1-8(13)5-9(7)10/h1-2,4-6,11,13H,3H2

Synthesis Reference

Marchand, B.; Streffer, Ch. Synthesis of 5-hydroxy-3-indolylacetaldehyde. Angew. Chem. (1959), 71 575.

Melting Point (Experimental)

Not Available

Experimental Water Solubility

Not Available Source: PhysProp

Predicted Water Solubility

1.32 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS

Physiological Charge

State

Solid

Experimental LogP/Hydrophobicity

Not Available Source: PhysProp

Predicted LogP/Hydrophobicity

1.93 [Predicted by ALOGPS]; 1.5 [Predicted by PubChem via XLOGP] Calculated using ALOGPS

Material Safety Data Sheet (MSDS)

Not Available

MOL File

Show

SDF File

Show

PDB File

Show

2D Structure

3D Structure

Experimental PDB ID

Not Available

Experimental ¹H NMR Spectrum

Not Available

Experimental ¹³C NMR Spectrum

Not Available

Experimental ¹³C HSQC Spectrum

Not Available

Predicted ¹H NMR Spectrum

Show Image
Show Peaklist

Predicted ¹³C NMR Spectrum

Show Image
Show Peaklist

Mass Spectrum

Not Available

Simplified TOCSY Spectrum

Not Available

BMRB Spectrum

Not Available

Cellular Location

Cytoplasm
mitochondria

Biofluid Location

Not Available

Tissue Location

Not Available

Concentrations (Normal)

Not Available

Concentrations (Abnormal)

Not Available

Associated Disorders

Not Available

OMIM ID

Not Available

Pathways

Name	SMPDB Link	KEGG Link
Tryptophan Metabolism	SMP00063	map00380

General References

Not Available

Metabolic Enzymes

Enzyme 1 [top]

Enzyme 1 ID

5358

Enzyme 1 Name

Aldehyde oxidase

Enzyme 1 Synonyms

Not Available

Enzyme 1 Gene Name

AOX1

Enzyme 1 Protein Sequence

>Aldehyde oxidase

MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTPYGCGGGGCGACTVMISRYN
PITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPG
MVMSIYPLLRNHPEPTLDQLTDALGGNLCRCHGYRPIIDACKTFCKTSGCCQSKENGVCC
LDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMADKQSQRTRVFGSER
MMWFSPVTLKDLLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPGYNSPDRIEEPECCKPC
IYGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHII
SRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPISR
KWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKL
IGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPV
HYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYC
DDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAE
KFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPE
RKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKY
IQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGE
DMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKF
PNLRCRGWACRTNLPSNTAFRGFGFPQAVLITESCITEVAAKCGLSPEKVRIINMYKEID
QTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLAS
RAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETV
PNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVG
YFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAID
IGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSN
TLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFT
KMIPRDEPGSYVPWNVPI

Enzyme 1 Number of Residues

1338

Enzyme 1 Molecular Weight

147933

Enzyme 1 Theoretical pI

7.11

Enzyme 1 GO Classification

Function
binding catalytic activity cation binding electron transporter activity ion binding iron ion binding metal ion binding oxidoreductase activity transition metal ion binding transporter activity
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
—

Enzyme 1 General Function

Nucleotide transport and metabolism

Enzyme 1 Specific Function

An aldehyde + H(2)O + O(2) = a carboxylic acid + H(2)O(2)

Enzyme 1 Pathways

Nicotinate and Nicotinamide Metabolism (map00760 )
Tryptophan Metabolism (map00380 )
Tyrosine Metabolism (map00350 )
Valine, Leucine and Isoleucine Degradation (map00280 )
Vitamin B6 Metabolism (map00750 )

Enzyme 1 Reactions

an aldehyde + H2O + O2 = a carboxylic acid + H2O2

Enzyme 1 Pfam Domain Function

Ald_Xan_dh_C (PF01315 )
Ald_Xan_dh_C2 (PF02738 )
CO_deh_flav_C (PF03450 )
FAD_binding_5 (PF00941 )
Fer2 (PF00111 )
Fer2_2 (PF01799 )

Enzyme 1 Signals

None

Enzyme 1 Transmembrane Regions

None

Enzyme 1 Essentiality

Not Available

Enzyme 1 GenBank ID Protein

438656

Enzyme 1 UniProtKB/Swiss-Prot ID

Q06278

Enzyme 1 UniProtKB/Swiss-Prot Entry Name

ADO_HUMAN

Enzyme 1 PDB ID

Not Available

Enzyme 1 Cellular Location

Not Available

Enzyme 1 Gene Sequence

>4017 bp

ATGGACCGGGCGTCCGAGCTGCTCTTCTACGTGAACGGCCGCAAGGTGATAGAAAAAAAT
GTCGATCCTGAAACAATGCTGTTGCCTTATTTGAGGAAGAAGCTTCGACTCACAGGAACT
CCGTATGGCTGTGGAGGAGGAGGCTGTGGTGCTTGTACAGTGATGATATCACGATACAAC
CCCATCACCAAGAGGATAAGGCATCACCCAGCCAATGCCTGTCTGATTCCCATCTGTTCT
CTGTATGGTGCTGCCGTCACCACAGTAGAAGGCATAGGAAGCACCCACACCAGAATTCAT
CCTGTTCAGGAGAGGATTGCCAAGTGTCATGGCACCCAGTGTGGCTTCTGCACACCTGGG
ATGGTGATGTCCATCTACCCCCTGCTCAGGAACCACCCAGAGCCCACTCTGGATCAGTTA
ACTGATGCCCTTGGTGGTAACCTGTGCCGTTGCCATGGATACAGGCCCATAATTGATGCA
TGCAAGACTTTCTGTAAAACTTCGGGCTGCTGTCAAAGTAAAGAAAATGGGGTTTGCTGT
TTGGATCAAGGAATCAATGGATTGCCAGAATTTGAGGAAGGAAGTAAGACAAGTCCAAAA
CTCTTCGCAGAAGAGGAGTTTCTGCCATTGGATCCAACCCAGGAACTGATATTTCCTCCT
GAGCTAATGATAATGGCTGATAAACAGTCGCAAAGGACCAGGGTGTTTGGCAGTGAGAGA
ATGATGTGGTTTTCCCCCGTGACCCTGAAGGACCTGCTGGAATTTAAATTCAAGTATCCC
CAGGCTCCTGTTATCATGGGAAACACCTCTGTGGGGCCTGAAGTGAAATTTAAAGGCGTC
TTTCACCCAGGTTATAATTCTCCTGATAGAATTGAAGAACCTGAGTGTTGTAAACCATGC
ATATATGGACTCACCCTTGGTGCTGGTCTCAGCCTAGCCCAGGTGAAGGACATTTTGGCT
GATGTAGTCCAGAAGCTTCCAGAGGAGAAGACACAGATGTACCATGCTCTCCTGAAGCAT
TTGGGAACTCTGGCTGGGTCCCAGATCAGGAACATGGCTTCTTTAGGGGGACACATCATT
AGCAGGCATCCAGATTCAGATCTGAATCCCATCCTGGCTGTGGGTAACTGTACCCTCAAC
TTGCTATCAAAAGAAGGAAAACGACAGATTCCTTTAAATGAGCAATTCCTCAGCAAGTGC
CCTAATGCAGATCTTAAGCCTCAAGAAATCTTGGTCTCAGTGAACATCCCCATCTCAAGG
AAGTGGGAATTTGTGTCAGCCTTCCGACAAGCCCAGCGACAGGAGAATGCGCTAGCGATA
GTCAATTCAGGAATGAGAGTCTTTTTTGGAGAAGGGGATGGCATTATTAGAGAGTTATGC
ATCTCATATGGAGGCGTTGGTCCAGCCACCATCTGTGCCAAGAATTCCTGCCAGAAACTC
ATTGGAAGGCACTGGAACGAACAGATGCTGGATATAGCCTGCAGGCTTATTCTGAATGAA
GTCTCCCTTTTGGGCTCGGCGCCAGGTGGGAAAGTGGAGTTCAAGAGGACTCTCATCATC
AGCTTCCTCTTCAAGTTCTACCTGGAAGTGTCACAGATTTTGAAAAAGATGGATCCAGTT
CACTATCCTAGCCTTGCAGACAAGTATGAAAGTGCTTTAGAAGATCTTCATTCCAAACAT
CACTGCAGTACATTAAAGTACCAGAATATAGGCCCAAAGCAGCATCCTGAAGACCCAATT
GGCCACCCCATCATGCATCTGTCTGGTGTGAAGCATGCCACGGGGGAGGCCATCTACTGT
GATGACATGCCTCTGGTGGACCAGGAACTTTTCTTGACTTTTGTGACTAGTTCAAGAGCT
CATGCTAAGATTGTGTCTATTGATCTGTCAGAAGCTCTCAGCATGCCCGGTGTGGTGGAC
ATCATGACAGCAGAACATCTTAGTGACGTCAACTCCTTCTGCTTTTTTACTGAAGCTGAG
AAATTTCTGGCGACAGATAAGGTGTTCTGTGTGGGTCAGCTTGTCTGTGCTGTGCTTGCC
GATTCTGAGGTTCAGGCAAAGCGAGCTGCTAAGCGAGTGAAGATTGTCTATCAAGACTTG
GAGCCGCTGATACTAACAATTGAGGAAAGTATACAACACAACTCCTCCTTCAAGCCAGAA
AGGAAACTGGAATATGGAAATGTTGACGAAGCATTTAAAGTGGTTGATCAAATTCTTGAA
GGTGAAATACATATGGGAGGTCAAGAACATTTTTATATGGAAACCCAAAGCATGCTTGTC
GTTCCCAAGGGAGAGGATCAAGAAATGGATGTCTACGTGTCCACACAGTTTCCCAAATAT
ATACAGGACATTGTTGCCTCAACCTTGAAGCTCCCAGCTAACAAGGTCATGTGCCATGTA
AGGCGTGTTGGTGGAGCGTTTGGAGGGAAGGTGTTAAAAACCGGAATCATTGCAGCCGTC
ACTGCATTTGCCGCAAACAAACATGGCCGTGCAGTTCGCTGTGTTCTGGAACGAGGAGAA
GACATGTTAATAACTGGAGGCCGCCATCCTTACCTTGGAAAGTACAAAGCTGGATTCATG
AACGATGGCAGAATCTTGGCCCTGGACATGGAGCATTACAGCAATGCAGGCGCCTCCTTG
GATGAATCATTATTCGTGATAGAAATGGGACTTCTGAAAATGGACAATGCTTACAAGTTT
CCCAATCTCCGCTGCCGGGGTTGGGCATGCAGAACCAACCTTCCATCCAACACAGCTTTT
CGTGGGTTTGGCTTTCCTCAGGCAGTGCTGATCACCGAATCTTGTATCACGGAAGTTGCA
GCCAAATGTGGACTATCCCCTGAGAAGGTGCGAATCATAAACATGTACAAGGAAATTGAT
CAAACACCCTACAAACAAGAGATCAATGCCAAGAACCTAATCCAGTGTTGGAGAGAATGT
ATGGCCATGTCTTCCTACTCCTTGAGGAAAGTTGCTGTGGAAAAGTTCAATGCAGAGAAT
TATTGGAAGAAGAAAGGACTGGCCATGGTCCCCCTGAAGTTTCCTGTTGGCCTTGCGTCA
CGTGCTGCTGGTCAGGCTGCTGCCTTGGTTCACATTTATCTTGATGGCTCTGTGCTGGTC
ACTCACGGTGGAATTGAAATGGGGCAGGGGGTCCACACTAAAATGATTCAGGTGGTCAGC
CGTGAATTAAGAATGCCAATGTCGAATGTCCACCTGCGTGGAACAAGCACAGAAACTGTC
CCTAATGCAAATATCTCTGGAGGTTCTGTGGTGGCAGATCTCAACGGTTTGGCAGTAAAG
GATGCCTGTCAAACTCTTCTAAAACGCCTCGAACCCATCATCAGCAAGAATCCTAAAGGA
ACTTGGAAAGACTGGGCACAGACTGCTTTTGATGAAAGCATTAACCTTTCAGCTGTTGGA
TACTTCAGAGGTTATGAGTCAGACATGAACTGGGAGAAAGGCGAAGGCCAGCCCTTCGAA
TACTTTGTTTATGGAGCTGCCTGTTCCGAGGTTGAAATAGACTGCCTGACGGGGGATCAT
AAGAACATCAGAACAGACATTGTCATGGATGTTGGCTGCAGTATAAATCCAGCCATTGAC
ATAGGCCAGATTGAAGGTGCATTTATTCAAGGCATGGGACTTTATACAATAGAGGAACTG
AATTATTCTCCCCAGGGCATTCTGCACACTCGTGGTCCAGACCAATATAAAATCCCTGCC
ATCTGTGACATGCCCACGGAGTTGCACATTGCTTTGTTGCCTCCTTCTCAAAACTCAAAT
ACTCTTTATTCATCTAAGGGTCTGGGAGAGTCGGGGGTGTTCCTGGGGTGTTCCGTGTTT
TTCGCTATCCATGACGCAGTGAGTGCAGCACGACAGGAGAGAGGCCTGCATGGACCCTTG
ACCCTTAATAGTCCACTGACCCCGGAGAAGATTAGGATGGCCTGTGAAGACAAGTTCACA
AAAATGATTCCGAGAGATGAACCTGGATCCTACGTTCCTTGGAATGTACCCATCTGA

Enzyme 1 GenBank Gene ID

Enzyme 1 GeneCard ID

Enzyme 1 GenAtlas ID

Enzyme 1 HGNC ID

Enzyme 1 Chromosome Location

Enzyme 1 Locus

2q33

Enzyme 1 SNPs

SNPJam Report Link Image

Enzyme 1 General References

Wright RM, Vaitaitis GM, Wilson CM, Repine TB, Terada LS, Repine JE: cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10690-4. [PubMed ]

Enzyme 1 Metabolite References

Not Available

Enzyme 2 [top]

Enzyme 2 ID

5401

Enzyme 2 Name

Amine oxidase [flavin-containing] A

Enzyme 2 Synonyms

Monoamine oxidase type A
MAO-A

Enzyme 2 Gene Name

MAOA

Enzyme 2 Protein Sequence

>Amine oxidase [flavin-containing] A

MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHV
DYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIA
YLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNI
NVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKL
NHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPM
GAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADR
LAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYG
RVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKD
VPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS

Enzyme 2 Number of Residues

527

Enzyme 2 Molecular Weight

59682

Enzyme 2 Theoretical pI

7.96

Enzyme 2 GO Classification

Function
catalytic activity oxidoreductase activity
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
—

Enzyme 2 General Function

Amino acid transport and metabolism

Enzyme 2 Specific Function

Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine

Enzyme 2 Pathways

Arginine and Proline Metabolism (map00330 )
Glycine, Serine and Threonine Metabolism (map00260 )
Histidine Metabolism (map00340 )
Phenylalanine Metabolism (map00360 )
Tryptophan Metabolism (map00380 )
Tyrosine Metabolism (map00350 )

Enzyme 2 Reactions

RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2

Enzyme 2 Pfam Domain Function

Amino_oxidase (PF01593 )

Enzyme 2 Signals

None

Enzyme 2 Transmembrane Regions

498-518

Enzyme 2 Essentiality

Not Available

Enzyme 2 GenBank ID Protein

187353

Enzyme 2 UniProtKB/Swiss-Prot ID

P21397

Enzyme 2 UniProtKB/Swiss-Prot Entry Name

AOFA_HUMAN Link Image

Enzyme 2 PDB ID

1O5W

Enzyme 2 PDB File

Show

Enzyme 2 3D Structure

Enzyme 2 Cellular Location

Not Available

Enzyme 2 Gene Sequence

>1584 bp

ATGGAGAATCAAGAGAAGGCGAGTATCGCGGGCCACATGTTCGACGTAGTCGTGATCGGA
GGTGGCATTTCAGGACTATCTGCTGCCAAACTCTTGACTGAATATGGCGTTAGTGTTTTG
GTTTTAGAAGCTCGGGACAGGGTTGGAGGAAGAACATATACTATAAGGAATGAGCATGTT
GATTACGTAGATGTTGGTGGAGCTTATGTGGGACCAACCCAAAACAGAATCTTACGCTTG
TCTAAGGAGCTGGGCATAGAGACTTACAAAGTGAATGTCAGTGAGCGTCTCGTTCAATAT
GTCAAGGGGAAAACATATCCATTTCGGGGCGCCTTTCCACCAGTATGGAATCCCATTGCA
TATTTGGATTACAATAATCTGTGGAGGACAATAGATAACATGGGGAAGGAGATTCCAACT
GATGCACCCTGGGAGGCTCAACATGCTGACAAATGGGACAAAATGACCATGAAAGAGCTC
ATTGACAAAATCTGCTGGACAAAGACTGCTAGGCGGTTTGCTTATCTTTTTGTGAATATC
AATGTGACCTCTGAGCCTCACGAAGTGTCTGCCCTGTGGTTCTTGTGGTATGTGAAGCAG
TGCGGGGGCACCACTCGGATATTCTCTGTCACCAATGGTGGCCAGGAACGGAAGTTTGTA
GGTGGATCTGGTCAAGTGAGCGAACGGATAATGGACCTCCTCGGAGACCAAGTGAAGCTG
AACCATCCTGTCACTCACGTTGACCAGTCAAGTGACAACATCATCATAGAGACGCTGAAC
CATGAACATTATGAGTGCAAATACGTAATTAATGCGATCCCTCCGACCTTGACTGCCAAG
ATTCACTTCAGACCAGAGCTTCCAGCAGAGAGAAACCAGTTAATTCAGCGGCTTCCAATG
GGAGCTGTCATTAAGTGCATGATGTATTACAAGGAGGCCTTCTGGAAGAAGAAGGATTAC
TGTGGCTGCATGATCATTGAAGATGAAGATGCTCCAATTTCAATAACCTTGGATGACACC
AAGCCTGATGGGTCACTGCCTGCCATCATGGGCTTCATTCTTGCCCGGAAAGCTGATCGA
CTTGCTAAGCTACATAAGGAAATAAGGAAGAAGAAAATCTGTGAGCTCTATGCCAAAGTG
CTGGGATCCCAAGAAGCTTTACATCCAGTGCATTATGAAGAGAAGAACTGGTGTGAGGAG
CAGTACTCTGGGGGCTGCTACACGGCCTACTTCCCTCCTGGGATCATGACTCAATATGGA
AGGGTGATTCGTCAACCCGTGGGCAGGATTTTCTTTGCGGGCACAGAGACTGCCACAAAG
TGGAGCGGCTACATGGAAGGGGCAGTTGAGGCTGGAGAACGAGCAGCTAGGGAGGTCTTA
AATGGTCTCGGGAAGGTGACCGAGAAAGATATCTGGGTACAAGAACCTGAATCAAAGGAC
GTTCCAGCGGTAGAAATCACCCACACCTTCTGGGAAAGGAACCTGCCCTCTGTTTCTGGC
CTGCTGAAGATCATTGGATTTTCCACATCAGTAACTGCCCTGGGGTTTGTGCTGTACAAA
TACAAGCTCCTGCCACGGTCTTGA

Enzyme 2 GenBank Gene ID

Enzyme 2 GeneCard ID

Enzyme 2 GenAtlas ID

Enzyme 2 HGNC ID

Enzyme 2 Chromosome Location

Enzyme 2 Locus

Xp11.3

Enzyme 2 SNPs

SNPJam Report Link Image

Enzyme 2 General References

Hsu YP, Weyler W, Chen S, Sims KB, Rinehart WB, Utterback MC, Powell JF, Breakefield XO: Structural features of human monoamine oxidase A elucidated from cDNA and peptide sequences. J Neurochem. 1988 Oct;51(4):1321-4. [PubMed ]
Bach AW, Lan NC, Johnson DL, Abell CW, Bembenek ME, Kwan SW, Seeburg PH, Shih JC: cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4934-8. [PubMed ]
Zhu QS, Grimsby J, Chen K, Shih JC: Promoter organization and activity of human monoamine oxidase (MAO) A and B genes. J Neurosci. 1992 Nov;12(11):4437-46. [PubMed ]
Denney RM: The promoter of the human monoamine oxidase A gene. Prog Brain Res. 1995;106:57-66. [PubMed ]
Denney RM, Sharma A, Dave SK, Waguespack A: A new look at the promoter of the human monoamine oxidase A gene: mapping transcription initiation sites and capacity to drive luciferase expression. J Neurochem. 1994 Sep;63(3):843-56. [PubMed ]
Chen SA, Weyler W: Partial amino acid sequence analysis of human placenta monoamine oxidase A and bovine liver monoamine oxidase B. Biochem Biophys Res Commun. 1988 Oct 14;156(1):445-50. [PubMed ]
Weyler W: Monoamine oxidase A from human placenta and monoamine oxidase B from bovine liver both have one FAD per subunit. Biochem J. 1989 Jun 15;260(3):725-9. [PubMed ]
Li M, Hubalek F, Newton-Vinson P, Edmondson DE: High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae. Protein Expr Purif. 2002 Feb;24(1):152-62. [PubMed ]

Enzyme 2 Metabolite References

Not Available

Enzyme 3 [top]

Enzyme 3 ID

5526

Enzyme 3 Name

4-trimethylaminobutyraldehyde dehydrogenase

Enzyme 3 Synonyms

TMABADH
Aldehyde dehydrogenase 9A1
Aldehyde dehydrogenase E3 isozyme
Gamma-aminobutyraldehyde dehydrogenase
R- aminobutyraldehyde dehydrogenase

Enzyme 3 Gene Name

ALDH9A1

Enzyme 3 Protein Sequence

>4-trimethylaminobutyraldehyde dehydrogenase

MSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRVIATFTCSGEKEVNLAVQNAKA
AFKIWSQKSGMERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYY
AGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFK
PSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSVPTGMKI
MEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEI
LDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIY
VPEDPKLKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLA
AGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQL
KTVCVEMGDVESAF

Enzyme 3 Number of Residues

494

Enzyme 3 Molecular Weight

53802

Enzyme 3 Theoretical pI

5.61

Enzyme 3 GO Classification

Function
catalytic activity oxidoreductase activity
Process
metabolism physiological process
Component
—

Enzyme 3 General Function

Energy production and conversion

Enzyme 3 Specific Function

Converts gamma-trimethylaminobutyraldehyde into gamma- butyrobetaine. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction

Enzyme 3 Pathways

Lysine Degradation (map00310 )

Enzyme 3 Reactions

4-trimethylammoniobutanal + NAD+ = 4-trimethylammoniobutanoate + NADH + H+

Enzyme 3 Pfam Domain Function

Aldedh (PF00171 )

Enzyme 3 Signals

None

Enzyme 3 Transmembrane Regions

None

Enzyme 3 Essentiality

Not Available

Enzyme 3 GenBank ID Protein

1049219

Enzyme 3 UniProtKB/Swiss-Prot ID

P49189

Enzyme 3 UniProtKB/Swiss-Prot Entry Name

AL9A1_HUMAN Link Image

Enzyme 3 PDB ID

Not Available

Enzyme 3 Cellular Location

Not Available

Enzyme 3 Gene Sequence

>1482 bp

ATGAGCACTGGCACCTTCGTCGTGTCGCAGCCGCTCAATTACCGCGGCGGGGCCGCTGGA
GCCGGCGGACGCTCCGGTACCGAGAAAGCTTTCGAGCCAGCAACCGGCCGAGTGATAGCT
ACTTTCACATGTTCAGGAGAAAAGGAAGTAAATTTGGCTGTTCAAAATGCAAAGGCTGCT
TTTAAAATATGGAGTCAAAAATCTGGCATGGAGCGTTGCCGAATCCTTTTGGAGGCTGCC
AGGATAATAAGGGAACGGGAGGATGAAATTGCTACTATGGAGTGCATCAACAATGGCAAG
TCCATCTTTGAGGCCCGCTTGGACATTGACATTTCCTGGCAGTGCCTGGAGTATTATGCG
GGCTTGGCTGCATCCATGGCTGGTGAACACATCCAGCTCCCAGGTGGATCGTTTGGTTAT
ACCAGAAGAGAACCACTTGGGGTATGTGTGGGAATAGGAGCATGGAACTACCCCTTTCAG
ATTGCCTCTTGGAAGTCGGCTCCAGCATTAGCCTGTGGTAATGCCATGGTCTTTAAACCT
TCTCCCTTTACACCTGTTTCTGCATTGCTACTGGCTGAAATCTACAGTGAGGCTGGTGTA
CCTCCTGGGCTCTTCAATGTGGTGCAGGGAGGGGCTGCCACAGGCCAGTTTCTGTGTCAG
CATCCCGATGTGGCCAAAGTCTCCTTCACTGGAAGTGTGCCCACTGGCATGAAGATCATG
GAGATGTCAGCTAAAGGAATCAAACCTGTTACCTTGGAACTTGGAGGCAAATCTCCACTC
ATCATCTTCTCAGACTGTGATATGAACAATGCTGTAAAGGGGGCGCTGATGGCCAACTTC
CTCACACAAGGCCAGGTTTGCTGTAATGGCACAAGAGTATTTGTGCAGAAAGAAATTCTT
GATAAATTTACAGAGGAAGTGGTGAAACAGACCCAAAGGATTAAAATTGGAGATCCCCTT
CTGGAAGATACAAGGATGGGTCCACTCATCAACCGACCACACCTGGAGCGAGTCCTTGGG
TTTGTCAAAGTGGCAAAGGAGCAGGGTGCTAAAGTGTTATGTGGTGGAGATATATATGTA
CCTGAAGATCCCAAATTAAAGGATGGATATTACATGAGACCTTGTGTATTAACTAATTGC
AGAGACGACATGACCTGTGTGAAGGAAGAGATCTTTGGGCCTGTTATGTCCATTTTATCA
TTTGACACTGAAGCTGAGGTTCTAGAAAGAGCCAATGATACCACTTTTGGACTAGCAGCT
GGCGTCTTTACCAGGGACATCCAACGGGCTCATAGAGTGGTAGCTGAGCTTCAGGCTGGG
ACGTGCTTCATTAACAACTATAACGTCAGCCCAGTGGAGTTGCCCTTTGGTGGATATAAG
AAGTCAGGATTTGGCAGAGAGAACGGCCGTGTGACAATCGAATATTATTCACAGCTGAAG
ACTGTGTGTGTGGAGATGGGTGATGTGGAATCTGCTTTTTGA

Enzyme 3 GenBank Gene ID

Enzyme 3 GeneCard ID

Enzyme 3 GenAtlas ID

Enzyme 3 HGNC ID

Enzyme 3 Chromosome Location

Enzyme 3 Locus

1q23.1

Enzyme 3 SNPs

SNPJam Report Link Image

Enzyme 3 General References

Lin SW, Chen JC, Hsu LC, Hsieh CL, Yoshida A: Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression. Genomics. 1996 Jun 15;34(3):376-80. [PubMed ]
Vaz FM, Fouchier SW, Ofman R, Sommer M, Wanders RJ: Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. J Biol Chem. 2000 Mar 10;275(10):7390-4. [PubMed ]
Kikonyogo A, Pietruszko R: Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution. Biochem J. 1996 May 15;316 ( Pt 1):317-24. [PubMed ]
Kurys G, Shah PC, Kikonygo A, Reed D, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde. Eur J Biochem. 1993 Dec 1;218(2):311-20. [PubMed ]
Kurys G, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde. J Biol Chem. 1989 Mar 15;264(8):4715-21. [PubMed ]

Enzyme 3 Metabolite References

Not Available

Enzyme 4 [top]

Enzyme 4 ID

5528

Enzyme 4 Name

Alpha-aminoadipic semialdehyde dehydrogenase

Enzyme 4 Synonyms

Alpha-AASA dehydrogenase
Delta1-piperideine-6-carboxylate dehydrogenease
P6c dehydrogenase
Aldehyde dehydrogenase family 7 member A1
Antiquitin-1

Enzyme 4 Gene Name

ALDH7A1

Enzyme 4 Protein Sequence

>Alpha-aminoadipic semialdehyde dehydrogenase

MSTLLINQPQYAWLKELGLREENEGVYNGSWGGRGEVITTYCPANNEPIARVRQASVADY
EETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQ
EYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIA
MICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVN
LLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQ
RCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEA
KKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWN
NEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES
GSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ

Enzyme 4 Number of Residues

511

Enzyme 4 Molecular Weight

55367

Enzyme 4 Theoretical pI

6.86

Enzyme 4 GO Classification

Function
catalytic activity oxidoreductase activity
Process
metabolism physiological process
Component
—

Enzyme 4 General Function

Energy production and conversion

Enzyme 4 Specific Function

L-2-aminoadipate 6-semialdehyde + NAD(P)(+) + H(2)O = L-2-aminoadipate + NAD(P)H

Enzyme 4 Pathways

Lysine Biosynthesis (map00300 )
Lysine Degradation (map00310 )

Enzyme 4 Reactions

L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

Enzyme 4 Pfam Domain Function

Aldedh (PF00171 )

Enzyme 4 Signals

None

Enzyme 4 Transmembrane Regions

None

Enzyme 4 Essentiality

Not Available

Enzyme 4 GenBank ID Protein

797410

Enzyme 4 UniProtKB/Swiss-Prot ID

P49419

Enzyme 4 UniProtKB/Swiss-Prot Entry Name

AL7A1_HUMAN Link Image

Enzyme 4 PDB ID

Not Available

Enzyme 4 Cellular Location

Not Available

Enzyme 4 Gene Sequence

>1536 bp

ATGTCCACTCTCCTCATCAATCAGCCCCAGTATGCGTGGCTGAAAGAGCTGGGGCTCCGC
GAGGAAAACGAGGGCGTGTATAATGGAAGCTGGGGAGGCCGGGGAGAGGTTATTACGACC
TATTGCCCCGCTAACAACGAGCCAATAGCAAGAGTCCGACAGGCCAGTGTGGCAGACTAT
GAAGAAACTGTAAAGAAAGCAAGAGAAGCATGGAAAATCTGGGCAGATATTCCTGCTCCA
AAACGAGGAGAAATAGTAAGACAGATTGGCGATGCCTTGCGGGAGAAGATCCAAGTACTA
GGAAGCTTGGTGTCTTTGGAGATGGGGAAAATCTTAGTGGAAGGTGTGGGTGAAGTTCAG
GAGTATGTGGATATCTGTGACTATGCTGTTGGTTTATCAAGGATGATTGGAGGACCTATC
TTGCCTTCTGAAAGATCTGGCCATGCACTGATTGAGCAGTGGAATCCCGTAGGCCTGGTT
GGAATCATCACGGCATTCAATTTCCCTGTGGCAGTGTATGGTTGGAACAACGCCATCGCC
ATGATCTGTGGAAATGTCTGCCTCTGGAAAGGAGCTCCAACCACTTCCCTCATTAGTGTG
GCTGTCACAAAGATAATAGCCAAGGTTCTGGAGGACAACAAGCTGCCTGGTGCAATTTGT
TCCTTGACTTGTGGTGGAGCAGATATTGGCACAGCAATGGCCAAAGATGAACGAGTGAAC
CTGCTGTCCTTCACTGGGAGCACTCAGGTGGGAAAACAGGTGGGCCTGATGGTGCAGGAG
AGGTTTGGGAGAAGTCTGTTGGAACTTGGAGGAAACAATGCCATTATTGCCTTTGAAGAT
GCAGACCTCAGCTTAGTTGTTCCATCAGCTCTCTTCGCTGCTGTGGGAACAGCTGGCCAG
AGGTGTACCACTGCGAGGCGACTGTTTATACATGAAAGCATCCATGATGAGGTTGTAAAC
AGACTTAAAAAGGCCTATGCACAGATCCGAGTTGGGAACCCATGGGACCCTAATGTTCTC
TATGGGCCACTCCACACCAAGCAGGCAGTGAGCATGTTTCTTGGAGCAGTGGAAGAAGCA
AAGAAAGAAGGTGGCACAGTGGTCTATGGGGGCAAGGTTATGGATCGCCCTGGAAATTAT
GTAGAACCGACAATTGTGACAGGTCTTGGCCACGATGCGTCCATTGCACACACAGAGACT
TTCGCTCCGATTCTCTATGTCTTTAAATTCAAGAATGAAGAAGAGGTCTTTGCATGGAAT
AATGAAGTAAAACAGGGACTTTCAAGTAGCATCTTTACCAAAGATCTGGGCAGAATCTTT
CGCTGGCTTGGACCTAAAGGATCAGACTGTGGCATTGTAAATGTCAACATTCCAACAAGT
GGGGCTGAGATTGGAGGTGCCTTTGGAGGAGAAAAGCACACTGGTGGTGGCAGGGAGTCT
GGCAGTGATGCCTGGAAACAGTACATGAGAAGGTCTACTTGTACTATCAACTACAGTAAA
GACCTTCCTCTGGCCCAAGGAATCAAGTTTCAGTAA

Enzyme 4 GenBank Gene ID

Enzyme 4 GeneCard ID

Enzyme 4 GenAtlas ID

Enzyme 4 HGNC ID

Enzyme 4 Chromosome Location

Enzyme 4 Locus

5q31

Enzyme 4 SNPs

SNPJam Report Link Image

Enzyme 4 General References

Lee P, Kuhl W, Gelbart T, Kamimura T, West C, Beutler E: Homology between a human protein and a protein of the green garden pea. Genomics. 1994 May 15;21(2):371-8. [PubMed ]
Skvorak AB, Robertson NG, Yin Y, Weremowicz S, Her H, Bieber FR, Beisel KW, Lynch ED, Beier DR, Morton CC: An ancient conserved gene expressed in the human inner ear: identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1). Genomics. 1997 Dec 1;46(2):191-9. [PubMed ]

Enzyme 4 Metabolite References

Not Available

Enzyme 5 [top]

Enzyme 5 ID

5529

Enzyme 5 Name

Aldehyde dehydrogenase 1A3

Enzyme 5 Synonyms

Aldehyde dehydrogenase 6
Retinaldehyde dehydrogenase 3
RALDH-3

Enzyme 5 Gene Name

ALDH1A3

Enzyme 5 Protein Sequence

>Aldehyde dehydrogenase 1A3

MATANGAVENGQPDRKPPALPRPIRNLEVKFTKIFINNEWHESKSGKKFATCNPSTREQI
CEVEEGDKPDVDKAVEAAQVAFQRGSPWRRLDALSRGRLLHQLADLVERDRATLAALETM
DTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPW
NFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTV
GAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVE
CAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQK
QFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPIL
KFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGF
KMSGNGRELGEYALAEYTEVKTVTIKLGDKNP

Enzyme 5 Number of Residues

512

Enzyme 5 Molecular Weight

56109

Enzyme 5 Theoretical pI

7.29

Enzyme 5 GO Classification

Function
catalytic activity oxidoreductase activity
Process
metabolism physiological process
Component
—

Enzyme 5 General Function

Energy production and conversion

Enzyme 5 Specific Function

Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Seems to be the key enzyme in the formation of an RA gradient along the dorso-ventral axis during the early eye development and also in the development of the olfactory system

Enzyme 5 Pathways

Gluconeogenesis (map00010 )
Histidine Metabolism (map00340 )
Phenylalanine Metabolism (map00360 )
Tyrosine Metabolism (map00350 )

Enzyme 5 Reactions

an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+

Enzyme 5 Pfam Domain Function

Aldedh (PF00171 )

Enzyme 5 Signals

None

Enzyme 5 Transmembrane Regions

None

Enzyme 5 Essentiality

Not Available

Enzyme 5 GenBank ID Protein

544482

Enzyme 5 UniProtKB/Swiss-Prot ID

P47895

Enzyme 5 UniProtKB/Swiss-Prot Entry Name

AL1A3_HUMAN Link Image

Enzyme 5 PDB ID

Not Available

Enzyme 5 Cellular Location

Not Available

Enzyme 5 Gene Sequence

>1539 bp

ATGGCCACCGCTAACGGGGCCGTGGAAAACGGGCAGCCGGACGGGAAGCCGCCGGCCCTG
CCGCGCCCCATCCGCAACCTGGAGGTCAAGTTCACCAAGATATTTATCAACAATGAATGG
CACGAATCCAAGAGTGGGAAAAAGTTTGCTACATGTAACCCTTCAACTCGGGAGCAAATA
TGTGAAGTGGAAGAAGGAGATAAGCCCGACGTGGACAAGGCTGTGGAGGCTGCACAGGTT
GCCTTCCAGAGGGGCTCGCCATGGCGCCGGCTGGATGCCCTGAGTCGTGGGCGGCTGCTG
CACCAGCTGGCTGACCTGGTGGAGAGGGACCGCGCCACCTTGGCCGCCCTGGAGACGATG
GATACAGGGAAGCCATTTCTTCATGCTTTTTTCATCGACCTGGAGGGCTGTATTAGAACC
CTCAGATACTTTGCAGGGTGGGCAGACAAAATCCAGGGCAAGACCATCCCCACAGATGAC
AACGTCGTATGCTTCACCAGGCATGAGCCCATTGGTGTCTGTGGGGCCATCACTCCATGG
AACTTCCCCCTGCTGATGCTGGTGTGGAAGCTGGCACCCGCCCTCTGCTGTGGGAACACC
ATGGTCCTGAAGCCTGCGGAGCAGACACCTCTCACCGCCCTTTATCTCGGCTCTCTGATC
AAAGAGGCCGGGTTCCCTCCAGGAGTGGTGAACATTGTGCCAGGATTCGGGCCCACAGTG
GGAGCAGCAATTTCTTCTCACCCTCAGATCAACAAGATCGCCTTCACCGGCTCCACAGAG
GTTGGAAAACTGGTTAAAGAAGCTGCGTCCCGGAGCAATCTGAAGCGGGTGACGCTGGAG
CTGGGGGGGAAGAACCCCTGCATCGTGTGTGCGGACGCTGACTTGGACTTGGCAGTGGAG
TGTGCCCATCAGGGAGTGTTCTTCAACCAAGGCCAGTGTTGCACGGCAGCCTCCAGGGTG
TTCGTGGAGGAGCAGGTCTACTCTGAGTTTGTCAGGCGGAGCGTGGAGTATGCCAAGAAA
CGGCCCGTGGGAGACCCCTTCGATGTCAAAACAGAACAGGGGCCTCAGATTGATCAAAAG
CAGTTCGACAAAATCTTAGAGCTGATCGAGAGTGGGAAGAAGGAAGGGGCCAAGCTGGAA
TGCGGGGGCTCAGCCATGGAAGACAAGGGGCTCTTCATCAAACCCACTGTCTTCTCAGAA
GTCACAGACAACATGCGGATTGCCAAAGAGGAGATTTTCGGGCCAGTGCAACCAATACTG
AAGTTCAAAAGTATCGAAGAAGTGATAAAAAGAGCGAATAGCACCGACTATGGACTCACA
GCAGCCGTGTTCACAAAAAATCTCGACAAAGCCCTGAAGTTGGCTTCTGCCTTAGAGTCT
GGAACGGTCTGGATCAACTGCTACAACGCCCTCTATGCACAGGCTCCATTTGGTGGCTTT
AAAATGTCAGGAAATGGCAGAGAACTAGGTGAATACGCTTTGGCCGAATACACAGAAGTG
AAAACTGTCACCATCAAACTTGGCGACAAGAACCCCTGA

Enzyme 5 GenBank Gene ID

Enzyme 5 GeneCard ID

Enzyme 5 GenAtlas ID

Enzyme 5 HGNC ID

Enzyme 5 Chromosome Location

Enzyme 5 Locus

15q26.3

Enzyme 5 SNPs

SNPJam Report Link Image

Enzyme 5 General References

Hsu LC, Chang WC, Hiraoka L, Hsieh CL: Molecular cloning, genomic organization, and chromosomal localization of an additional human aldehyde dehydrogenase gene, ALDH6. Genomics. 1994 Nov 15;24(2):333-41. [PubMed ]

Enzyme 5 Metabolite References

Not Available

Enzyme 6 [top]

Enzyme 6 ID

5530

Enzyme 6 Name

Aldehyde dehydrogenase, mitochondrial precursor

Enzyme 6 Synonyms

ALDH class 2
ALDHI
ALDH-E2

Enzyme 6 Gene Name

ALDH2

Enzyme 6 Protein Sequence

>Aldehyde dehydrogenase, mitochondrial precursor

MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPS
TGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLA
ALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCG
QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPG
FGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADM
DWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGP
QVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGP
VMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS
PFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS

Enzyme 6 Number of Residues

517

Enzyme 6 Molecular Weight

56382

Enzyme 6 Theoretical pI

7.05

Enzyme 6 GO Classification

Function
catalytic activity oxidoreductase activity
Process
metabolism physiological process
Component
—

Enzyme 6 General Function

Energy production and conversion

Enzyme 6 Specific Function

An aldehyde + NAD(+) + H(2)O = an acid + NADH

Enzyme 6 Pathways

1,2-Dichloroethane degradation (map00631 )
Arginine and Proline Metabolism (map00330 )
Ascorbate and aldarate metabolism (map00053 )
Beta Alanine Metabolism (map00410 )
Bile Acid Biosynthesis (map00120 )
Butyrate Metabolism (map00650 )
Fatty Acid Metabolism (map00071 )
Gluconeogenesis (map00010 )
Glycerolipid Metabolism (map00561 )
Histidine Metabolism (map00340 )
Limonene and pinene degradation (map00903 )
Lysine Degradation (map00310 )
Propanoate Metabolism (map00640 )
Pyruvate Metabolism (map00620 )
Tryptophan Metabolism (map00380 )
Valine, Leucine and Isoleucine Degradation (map00280 )

Enzyme 6 Reactions

an aldehyde + NAD+ + H2O = an acid + NADH + H+

Enzyme 6 Pfam Domain Function

Aldedh (PF00171 )

Enzyme 6 Signals

1-24

Enzyme 6 Transmembrane Regions

Not Available

Enzyme 6 Essentiality

Not Available

Enzyme 6 GenBank ID Protein

28606

Enzyme 6 UniProtKB/Swiss-Prot ID

P05091

Enzyme 6 UniProtKB/Swiss-Prot Entry Name

ALDH2_HUMAN Link Image

Enzyme 6 PDB ID

1OF7

Enzyme 6 PDB File

Show

Enzyme 6 3D Structure

Enzyme 6 Cellular Location

Not Available

Enzyme 6 Gene Sequence

>1551 bp

ATGTTGCGCGCTGCCGCCGCTCGGGCCCCGCCTGGCCGCCGCCTCTTGTCAGCCGCCGCC
ACCCAGGCCGTGCCTGCCCCCAACCAGCAGCCCGAGGTCTTCTGCAACCAGATTTTCATA
AACAATGAATGGCACGATGCCGTCAGCAGGAAAACATTCCCCACCGTCAATCCGTCCACT
GGAGAGGTCATCTGTCAGGTAGCTGAAGGGGACAAGGAAGATGTGGACAAGGCACGTGAA
GGCCGCCCGGGCGCCTTCCAGCTGGGCTCACCTTGGCGCCGCATGGACGCATCACACAGC
GGCCGGCTGCTGAACCGCCTGGCCGATCTGATCGAGCGGGACCGGACCTACCTGGCGGCC
TTGGAGACCCTGGACAATGGCAAGCCCTATGTCATCTCCTACCTGGTGGATTTGGACATG
GTCCTCAAATGTCTCCGGTATTATGCCGGCTGGGCTGATAAGTACCACGGGAAAACCATC
CCCATTGACGGAGACTTCTTCAGCTACACACGCCATGAACCTGTGGGGGTGTGCGGGCAG
ATCATTCCGTGGAATTTCCCGCTCCTGATGCAAGCATGGAAGCTGGGCCCAGCCTTGGCA
ACTGGAAACGTGGTTGTGATGAAGGTAGCTGAGCAGACACCCCTCACCGCCCTCTATGTG
GCCAACCTGATCAAGGAGGCTGGCTTTCCCCCTGGTGTGGTCAACATTGTGCCTGGATTT
GGCCCCACGGCTGGGGCCGCCATTGCCTCCCATGAGGATGTGGACAAAGTGGCATTCACA
GGCTCCACTGAGATTGGCCGCGTAATCCAGGTTGCTGCTGGGAGCAGCAACCTCAAGAGA
GTGACCTTGGAGCTGGGGGGGAAGAGCCCCAACATCATCATGTCAGATGCCGATATGGAT
TGGGCCGTGGAACAGGCCCACTTCGCCCTGTTCTTCAACCAGGGCCAGTGCTGCTGTGCC
GGCTCCCGGACCTTCGTGCAGGAGGACATCTATGATGAGTTTGTGGTGCGGAGCGTTGCC
CGGGCCAAGTCTCGGGTGGTCGGGAACCCCTTTGATAGCAAGACCGAGCAGGGGCCGCAG
GTGGATGAAACTCAGTTTAAGAAGATCCTCGGCTACATCAACACGGGGAAGCAAGAGGGG
GCGAAGCTGCTGTGTGGTGGGGGCATTGCTGCTGACCGTGGTTACTTCATCCAGCCCACT
GTGTTTGGAGATGTGCAGGATGGCATGACCATCGCCAAGGAGGAGATCTTCGGGCCAGTG
ATGCAGATCCTGAAGTTCAAGACCATAGAGGAGGTTGTTGGGAGAGCCAACAATTCCACG
TACGGGCTGGCCGCAGCTGTCTTCACAAAGGATTTGGACAAGGCCAATTACCTGTCCCAG
GCCCTCCAGGCGGGCACTGTGTGGGTCAACTGCTATGATGTGTTTGGAGCCCAGTCACCC
TTTGGTGGCTACAAGATGTCGGGGAGTGGCCGGGAGTTGGGCGAGTACGGGCTGCAGGCA
TACACTGAAGTGAAAACTGTCACAGTCAAAGTGCCTCAGAAGAACTCATAA

Enzyme 6 GenBank Gene ID

Enzyme 6 GeneCard ID

Enzyme 6 GenAtlas ID

Enzyme 6 HGNC ID

Enzyme 6 Chromosome Location

Enzyme 6 Locus

12q24.2

Enzyme 6 SNPs

SNPJam Report Link Image

Enzyme 6 General References

Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Evidence for a signal peptide at the amino-terminal end of human mitochondrial aldehyde dehydrogenase. FEBS Lett. 1987 May 11;215(2):233-6. [PubMed ]
Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Isolation and sequence analysis of a full length cDNA clone coding for human mitochondrial aldehyde dehydrogenase. Nucleic Acids Res. 1987 Apr 10;15(7):3179. [PubMed ]
Hsu LC, Bendel RE, Yoshida A: Genomic structure of the human mitochondrial aldehyde dehydrogenase gene. Genomics. 1988 Jan;2(1):57-65. [PubMed ]
Hempel J, Kaiser R, Jornvall H: Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations. Eur J Biochem. 1985 Nov 15;153(1):13-28. [PubMed ]
Hsu LC, Tani K, Fujiyoshi T, Kurachi K, Yoshida A: Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3771-5. [PubMed ]
Yoshida A, Ikawa M, Hsu LC, Tani K: Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases. Alcohol. 1985 Jan-Feb;2(1):103-6. [PubMed ]
Agarwal DP, Goedde HW: Human aldehyde dehydrogenase isozymes and alcohol sensitivity. Isozymes Curr Top Biol Med Res. 1987;16:21-48. [PubMed ]
Hempel J, Hoog JO, Jornvall H: Mitochondrial aldehyde dehydrogenase. Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data. FEBS Lett. 1987 Sep 28;222(1):95-8. [PubMed ]
Yoshida A, Huang IY, Ikawa M: Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals. Proc Natl Acad Sci U S A. 1984 Jan;81(1):258-61. [PubMed ]
Novoradovsky A, Tsai SJ, Goldfarb L, Peterson R, Long JC, Goldman D: Mitochondrial aldehyde dehydrogenase polymorphism in Asian and American Indian populations: detection of new ALDH2 alleles. Alcohol Clin Exp Res. 1995 Oct;19(5):1105-10. [PubMed ]
Ni L, Zhou J, Hurley TD, Weiner H: Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Sci. 1999 Dec;8(12):2784-90. [PubMed ]

Enzyme 6 Metabolite References

Not Available

Enzyme 7 [top]

Enzyme 7 ID

5531

Enzyme 7 Name

Fatty aldehyde dehydrogenase

Enzyme 7 Synonyms

Aldehyde dehydrogenase, microsomal
Aldehyde dehydrogenase family 3 member A2
Aldehyde dehydrogenase 10

Enzyme 7 Gene Name

ALDH3A2

Enzyme 7 Protein Sequence

>Fatty aldehyde dehydrogenase

MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQE
VITVLGEIDFMLENLPEWVTAKPVKKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQ
PLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELLKQRFDH
IFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQT
CIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKI
AFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLA
LYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFS
HQRPCLLKSLKREGANKLRYPPNSQSKVDWGKFFLLKRFNKEKLGLLLLTFLGIVAAVLV
KAEYY

Enzyme 7 Number of Residues

485

Enzyme 7 Molecular Weight

54849

Enzyme 7 Theoretical pI

7.99

Enzyme 7 GO Classification

Function
catalytic activity oxidoreductase activity
Process
metabolism physiological process
Component
—

Enzyme 7 General Function

Energy production and conversion

Enzyme 7 Specific Function

Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length

Enzyme 7 Pathways

1,2-Dichloroethane degradation (map00631 )
Arginine and Proline Metabolism (map00330 )
Ascorbate and aldarate metabolism (map00053 )
Beta Alanine Metabolism (map00410 )
Bile Acid Biosynthesis (map00120 )
Butyrate Metabolism (map00650 )
Fatty Acid Metabolism (map00071 )
Gluconeogenesis (map00010 )
Glycerolipid Metabolism (map00561 )
Histidine Metabolism (map00340 )
Limonene and pinene degradation (map00903 )
Lysine Degradation (map00310 )
Propanoate Metabolism (map00640 )
Pyruvate Metabolism (map00620 )
Tryptophan Metabolism (map00380 )
Valine, Leucine and Isoleucine Degradation (map00280 )

Enzyme 7 Reactions

an aldehyde + NAD+ + H2O = an acid + NADH + H+

Enzyme 7 Pfam Domain Function

Aldedh (PF00171 )

Enzyme 7 Signals

None

Enzyme 7 Transmembrane Regions

464-480

Enzyme 7 Essentiality

Not Available

Enzyme 7 GenBank ID Protein

1082036

Enzyme 7 UniProtKB/Swiss-Prot ID

P51648

Enzyme 7 UniProtKB/Swiss-Prot Entry Name

AL3A2_HUMAN Link Image

Enzyme 7 PDB ID

Not Available

Enzyme 7 Cellular Location

Not Available

Enzyme 7 Gene Sequence

>1458 bp

ATGGAGCTCGAAGTCCGGCGGGTCCGACAGGCGTTCCTGTCCGGCCGGTCGCGACCTCTG
CGGTTTCGGCTGCAGCAGCTGGAGGCCCTGCGGAGGATGGTGCAGGAGCGCGAGAAGGAT
ATCCTGACGGCCATCGCCGCCGACCTGTGCAAGAGTGAATTCAATGTGTACAGTCAGGAA
GTCATTACTGTCCTTGGGGAAATTGATTTTATGCTTGAGAATCTTCCTGAATGGGTTACT
GCTAAACCAGTTAAGAAGAACGTGCTCACCATGCTGGATGAGGCCTATATTCAGCCACAG
CCTCTGGGAGTGGTGCTGATAATCGGAGCTTGGAATTACCCCTTCGTTCTCACCATTCAG
CCACTGATAGGAGCCATCGCTGCAGGAAATGCTGTGATTATAAAGCCTTCTGAACTGAGT
GAAAATACAGCCAAGATCTTGGCAAAGCTTCTCCCTCAGTATTTAGACCAGGATCTCTAT
ATTGTTATTAATGGTGGTGTTGAGGAAACCACGGAGCTCCTGAAGCAGCGATTTGACCAC
ATTTTCTATACGGGAAACACTGCGGTTGGCAAAATTGTCATGGAAGCTGCTGCCAAGCAT
CTGACCCCTGTGACTCTTGAACTGGGAGGGAAAAGTCCATGTTATATTGATAAAGATTGT
GACCTGGACATTGTTTGCAGACGCATAACCTGGGGAAAATACATGAATTGTGGCCAAACC
TGCATTGCACCCGACTATATTCTCTGTGAAGCATCCCTCCAAAATCAAATTGTATGGAAG
ATTAAGGAAACAGTGAAGGAATTTTATGGAGAAAATATAAAAGAGTCTCCTGATTATGAA
AGGATCATCAATCTTCGTCATTTTAAGAGGATACTAAGTTTGCTTGAAGGACAAAAGATA
GCTTTTGGTGGGGAGACTGATGAGGCCACACGCTACATAGCCCCAACAGTACTTACCGAT
GTTGATCCTAAAACCAAGGTGATGCAAGAAGAAATTTTTGGACCAATTCTTCCAATAGTG
CCTGTGAAAAATGTAGATGAGGCCATAAATTTCATAAATGAACGTGAAAAGCCTCTGGCT
CTTTATGTATTTTCGCATAACCATAAGCTCATCAAACGGATGATTGATGAGACATCCAGT
GGAGGTGTCACAGGCAATGACGTCATTATGCACTTCACGCTCAACTCTTTCCCATTTGGA
GGAGTGGGTTCCAGTGGGATGGGAGCTTATCACGGAAAACATAGTTTTGATACTTTTTCT
CATCAGCGTCCCTGTTTATTAAAAAGTTTAAAGAGAGAAGGTGCTAACAAACTCAGATAT
CCTCCCAACAGCCAGTCAAAGGTGGATTGGGGGAAATTTTTTCTCTTGAAACGGTTCAAC
AAAGAAAAACTCGGTCTCCTGTTGCTCACTTTCCTGGGTATTGTAGCCGCTGTGCTTGTC
AAGGCAGAATATTACTGA

Enzyme 7 GenBank Gene ID

Enzyme 7 GeneCard ID

Enzyme 7 GenAtlas ID

Enzyme 7 HGNC ID

Enzyme 7 Chromosome Location

Enzyme 7 Locus

17p11.2

Enzyme 7 SNPs

SNPJam Report Link Image

Enzyme 7 General References

De Laurenzi V, Rogers GR, Hamrock DJ, Marekov LN, Steinert PM, Compton JG, Markova N, Rizzo WB: Sjogren-Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene. Nat Genet. 1996 Jan;12(1):52-7. [PubMed ]
Rogers GR, Markova NG, De Laurenzi V, Rizzo WB, Compton JG: Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH). Genomics. 1997 Jan 15;39(2):127-35. [PubMed ]
Chang C, Yoshida A: Human fatty aldehyde dehydrogenase gene (ALDH10): organization and tissue-dependent expression. Genomics. 1997 Feb 15;40(1):80-5. [PubMed ]
Sillen A, Jagell S, Wadelius C: A missense mutation in the FALDH gene identified in Sjogren-Larsson syndrome patients originating from the northern part of Sweden. Hum Genet. 1997 Aug;100(2):201-3. [PubMed ]
Sillen A, Anton-Lamprecht I, Braun-Quentin C, Kraus CS, Sayli BS, Ayuso C, Jagell S, Kuster W, Wadelius C: Spectrum of mutations and sequence variants in the FALDH gene in patients with Sjogren-Larsson syndrome. Hum Mutat. 1998;12(6):377-84. [PubMed ]

Enzyme 7 Metabolite References

Not Available

Enzyme 8 [top]

Enzyme 8 ID

5532

Enzyme 8 Name

Aldehyde dehydrogenase X, mitochondrial precursor

Enzyme 8 Synonyms

Aldehyde dehydrogenase family 1 member B1
ALDH class 2

Enzyme 8 Gene Name

ALDH1B1

Enzyme 8 Protein Sequence

>Aldehyde dehydrogenase X, mitochondrial precursor

MLRFLAPRLLSLQGRTARYSSAAALPSPILNPDIPYNQLFINNEWQDAVSKKTFPTVNPT
TGEVIGHVAEGDRADVDRAVKAAREAFRLGSPWRRMDASERGRLLNLLADLVERDRVYLA
SLETLDNGKPFQESYALDLDEVIKVYRYFAGWADKWHGKTIPMDGQHFCFTRHEPVGVCG
QIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITG
YGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGDSNLKRVTLELGGKSPSIVLADADM
EHAVEQCHEALFFNMGQCCCAGSRTFVEESIYNEFLERTVEKAKQRKVGNPFELDTQQGP
QVDKEQFERVLGYIQLGQKEGAKLLCGGERFGERGFFIKPTVFGGVQDDMRIAKEEIFGP
VQPLFKFKKIEEVVERANNTRYGLAAAVFTRDLDKAMYFTQALQAGTVWVNTYNIVTCHT
PFGGFKESGNGRELGEDGLKAYTEVKTVTIKVPQKNS

Enzyme 8 Number of Residues

517

Enzyme 8 Molecular Weight

57239

Enzyme 8 Theoretical pI

6.79

Enzyme 8 GO Classification

Function
catalytic activity oxidoreductase activity
Process
metabolism physiological process
Component
—

Enzyme 8 General Function

Energy production and conversion

Enzyme 8 Specific Function

ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation

Enzyme 8 Pathways

1,2-Dichloroethane degradation (map00631 )
Arginine and Proline Metabolism (map00330 )
Ascorbate and aldarate metabolism (map00053 )
Beta Alanine Metabolism (map00410 )
Bile Acid Biosynthesis (map00120 )
Butyrate Metabolism (map00650 )
Fatty Acid Metabolism (map00071 )
Gluconeogenesis (map00010 )
Glycerolipid Metabolism (map00561 )
Histidine Metabolism (map00340 )
Limonene and pinene degradation (map00903 )
Lysine Degradation (map00310 )
Propanoate Metabolism (map00640 )
Pyruvate Metabolism (map00620 )
Tryptophan Metabolism (map00380 )
Valine, Leucine and Isoleucine Degradation (map00280 )

Enzyme 8 Reactions

an aldehyde + NAD+ + H2O = an acid + NADH + H+

Enzyme 8 Pfam Domain Function

Aldedh (PF00171 )

Enzyme 8 Signals

1-22

Enzyme 8 Transmembrane Regions

Not Available

Enzyme 8 Essentiality

Not Available

Enzyme 8 GenBank ID Protein

1263008

Enzyme 8 UniProtKB/Swiss-Prot ID

P30837

Enzyme 8 UniProtKB/Swiss-Prot Entry Name

AL1B1_HUMAN Link Image

Enzyme 8 PDB ID

Not Available

Enzyme 8 Cellular Location

Not Available

Enzyme 8 Gene Sequence

>1554 bp

ATGCTGCGCTTCCTGGCACCCCGGCTGCTTAGCCTCCAGGGCAGGACCGCCCTCTACTCC
TCGGCAGCAGCCCTCCCAAGCCCCATTCTGAACCCAGACATCCCCTACAACCAGCTGTTC
ATCAACAATGAATGGCAAGATGCAGTCAGCAAGAAGACCTTCCCGACGGTCAACCCTACC
ACCGGGGAGGTCATCGGGCACGTGGCTGAAGGTGACCGGGCTGATGTGGATCGGGCCGTG
AAAGCAGCCCGGGAAGCCTTCCGCCTGGGGTCCCCATGGCGCCGGATGGATGCCTCTGAG
CGGGGCCGGCTGCTGAACCTCCTGGCAGACCTAGTGGAGCGGGATCGAGTCTACTTGGCC
TCACTCGAGACCTTGGACAATGGGAAGCCTTTCCAAGAGTCTTACGCCTTGGACTTGGAT
GAGGTCATCAAGGTGTATCGGTACTTTGCTGGCTGGGCTGACAAGTGGCATGGCAAGACC
ATCCCCATGCATGGCCAGCATTTCTGCTTCACCCGGCATGAGCCCGTTGGTGTCTGTGGC
CAGATCATCCCGTGGAACTTCCCCTTGGTCATGCAGGGTTGGAAACTTGCCCCGGCACTC
GCCACAGGCAACACTGTGGTTATGAAGGTGGCAGAGCAGACCCCCCTCTCTGCCCTGTAT
TTGGCCTCCCTCATCAAGGAGGCAGGCTTTCCCCCTGGGGTGGTGAACATCATCACGGGG
TATGGCCCAACAGCAGGTGCGGCCATCGCCCAGCACATGGATGTTGACAAAGTTGCCTTC
ACCGGTTCCACCGAGGTGGGCCACCTGATCCAGAAAGCAGCTGGCGATTCCAACCTCAAG
AGAGTCACCCTGGAGCTGGGTGGTAAGAGCCCCAGCATCGTGCTGGCCGATGCTGACATG
GAGCATGCCGTGGAGCAGTGCCACGAAGCCCTGTTCTTCAACATGGGCCAGTGCTGCTGT
GCTGGCTCCCGGACCTTCGTGGAAGAATCCATCTACAATGAGTTTCTCGAGAGAACCGTG
GAGAAAGCAAAGCAGAGGAAAGTGGGGAACCCCTTTGAGCTGGACACCCAGCAGGGGCCT
CAGGTGGACAAGGAGCAGTTTGAACGAGTCCTAGGCTACATCCAGCTTGGCCAGAAGGAG
GGCGCAAAACTCCTCTGTGGCGGAGAGCGTTTCGGGGAGCGTGGTTTCTTCATCAAGCCT
ACTGTCTTTGGTGGCGTGCAGGATGACATGAGAATTGCCAAAGAGGAGATCTTTGGGCCT
GTGCAGCCCCTGTTCAAGTTCAAGAAGATTGAGGAGGTGGTTGAGAGGGCCAACAACACC
AGGTATGGCCTGGCTGCGGCTGTGTTCACCCGGGATCTGGACAAGGCCATGTACTTCACC
CAGGCACTCCAGGCCGGGACCGTGTGGGTAAACACCTACAACATCGTCACCTGCCACACG
CCATTTGGAGGGTTTAAGGAATCTGGAAACGGGAGGGAGCTGGGTGAGGATGGGCTTAAG
GCCTACACAGAGGTAAAGACGGTCACCATCAAGGTTCCTCAGAAGAACTCGTAA

Enzyme 8 GenBank Gene ID

Enzyme 8 GeneCard ID

Enzyme 8 GenAtlas ID

Enzyme 8 HGNC ID

Enzyme 8 Chromosome Location

Enzyme 8 Locus

9p11.1

Enzyme 8 SNPs

SNPJam Report Link Image

Enzyme 8 General References

Hsu LC, Chang WC: Cloning and characterization of a new functional human aldehyde dehydrogenase gene. J Biol Chem. 1991 Jul 5;266(19):12257-65. [PubMed ]
Sherman D, Dave V, Hsu LC, Peters TJ, Yoshida A: Diverse polymorphism within a short coding region of the human aldehyde dehydrogenase-5 (ALDH5) gene. Hum Genet. 1993 Nov;92(5):477-80. [PubMed ]

Enzyme 8 Metabolite References

Not Available

Enzyme 9 [top]

Enzyme 9 ID

5652

Enzyme 9 Name

Indolethylamine N-methyltransferase

Enzyme 9 Synonyms

Aromatic alkylamine N-methyltransferase
Indolamine N-methyltransferase
Arylamine N- methyltransferase
Amine N-methyltransferase

Enzyme 9 Gene Name

INMT

Enzyme 9 Protein Sequence

>Indolethylamine N-methyltransferase

MKGGFTGGDEYQKHFLPRDYLATYYSFDGSPSPEAEMLKFNLECLHKTFGPGGLQGDTLI
DIGSGPTIYQVLAACDSFQDITLSDFTDRNREELEKWLKKEPGAYDWTPAVKFACELEGN
SGRWEEKEEKLRAAVKRVLKCDVHLGNPLAPAVLPLADCVLTLLAMECACCSLDAYRAAL
CNLASLLKPGGHLVTTVTLRLPSYVVGKREFSCVALEKEEVEQAVLDAGFDIEQLLHSPQ
SYSVTNAANNGVCCIVARKKPGP

Enzyme 9 Number of Residues

263

Enzyme 9 Molecular Weight

28815

Enzyme 9 Theoretical pI

4.92

Enzyme 9 GO Classification

Function
catalytic activity methyltransferase activity transferase activity transferase activity, transferring one-carbon groups
Process
—
Component
—

Enzyme 9 General Function

Not Available

Enzyme 9 Specific Function

Catalyzes the N-methylation of tryptamine and structurally related compounds (Potential)

Enzyme 9 Pathways

Tryptophan Metabolism (map00380 )

Enzyme 9 Reactions

S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine

Enzyme 9 Pfam Domain Function

NNMT_PNMT_TEMT (PF01234 )

Enzyme 9 Signals

None

Enzyme 9 Transmembrane Regions

None

Enzyme 9 Essentiality

Not Available

Enzyme 9 GenBank ID Protein

6580815

Enzyme 9 UniProtKB/Swiss-Prot ID

O95050

Enzyme 9 UniProtKB/Swiss-Prot Entry Name

INMT_HUMAN Link Image

Enzyme 9 PDB ID

Not Available

Enzyme 9 Cellular Location

Not Available

Enzyme 9 Gene Sequence

>792 bp

ATGAAGGGTGGCTTCACTGGGGGTGATGAGTACCAGAAGCACTTCCTGCCCAGGGACTAC
TTGGCTACTTACTACAGCTTCGATGGCAGCCCCTCACCCGAGGCCGAGATGCTGAAGTTT
AACTTGGAATGTCTCCACAAGACCTTCGGCCCTGGAGGCCTCCAAGGGGACACGCTGATT
GACATTGGCTCAGGTCCTACCATCTACCAAGTTCTTGCTGCCTGTGATTCCTTCCAAGAC
ATCACTCTCTCCGACTTTACCGACCGCAACCGGGAGGAGCTGGAAAAGTGGCTGAAGAAG
GAGCCGGGGGCCTATGACTGGACCCCAGCGGTGAAATTCGCCTGTGAGCTGGAAGGAAAC
AGCGGCCGATGGGAGGAGAAGGAGGAGAAGCTGCGGGCAGCGGTGAAGCGGGTGCTCAAG
TGCGATGTCCACCTGGGCAACCCGCTGGCCCCGGCTGTGTTGCCTCTCGCCGACTGTGTG
CTCACCCTGCTGGCCATGGAGTGTGCCTGCTGTAGCCTTGATGCCTACCGCGCTGCCCTG
TGCAACCTTGCCTCACTGCTCAAGCCGGGTGGCCACCTGGTGACCACTGTCACGCTTCGG
CTCCCGTCCTACGTGGTGGGGAAGCGTGAATTTTCCTGCGTGGCCCTGGAGAAAGAGGAG
GTGGAGCAGGCTGTCCTGGATGCTGGCTTTGACATTGAACAGCTCCTACACAGTCCCCAG
AGCTACTCTGTCACCAATGCTGCCAACAATGGGGTCTGCTGCATTGTGGCTCGCAAGAAG
CCTGGGCCCTGA

Enzyme 9 GenBank Gene ID

Enzyme 9 GeneCard ID

Enzyme 9 GenAtlas ID

Enzyme 9 HGNC ID

Enzyme 9 Chromosome Location

Not Available

Enzyme 9 Locus

Not Available

Enzyme 9 SNPs

SNPJam Report Link Image

Enzyme 9 General References

Thompson MA, Moon E, Kim UJ, Xu J, Siciliano MJ, Weinshilboum RM: Human indolethylamine N-methyltransferase: cDNA cloning and expression, gene cloning, and chromosomal localization. Genomics. 1999 Nov 1;61(3):285-97. [PubMed ]
Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]

Enzyme 9 Metabolite References

Not Available

Enzyme 10 [top]

Enzyme 10 ID

5714

Enzyme 10 Name

Protein arginine N-methyltransferase 3

Enzyme 10 Synonyms

Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3

Enzyme 10 Gene Name

PRMT3

Enzyme 10 Protein Sequence

>Protein arginine N-methyltransferase 3

MCSLASGATGGRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCLFCNRLFTSA
EETFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWEKEEY
LKPVLEDDLLLQFDVEDLYEPVSVPFSYPNGLSENTSVVEKLKHMEARALSAEAALARAR
EDLQKMKQFAQDFVMHTDVRTCSSSTSVIADLQEDEDGVYFSSYGHYGIHEEMLKDKIRT
ESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVLGVDQSEILYQAMDIIRLN
KLEDTITLIKGKIEEVHLPVEKVDVIISEWMGYFLLFESMLDSVLYAKNKYLAKGGSVYP
DICTISLVAVSDVNKHADRIAFWDDVYGFKMSCMKKAVIPEAVVEVLDPKTLISEPCGIK
HIDCHTTSISDLEFSSDFTLKITRTSMCTAIAGYFDIYFEKNCHNRVVFSTGPQSTKTHW
KQTVFLLEKPFSVKAGEALKGKVTVHKNKKDPRSLTVTLTLNNSTQTYGLQ

Enzyme 10 Number of Residues

531

Enzyme 10 Molecular Weight

59904

Enzyme 10 Theoretical pI

5.00

Enzyme 10 GO Classification

Function
binding cation binding ion binding nucleic acid binding transition metal ion binding zinc ion binding
Process
—
Component
intracellular membrane-bound organelle membrane-bound organelle nucleus organelle

Enzyme 10 General Function

Not Available

Enzyme 10 Specific Function

Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins

Enzyme 10 Pathways

Not Available

Enzyme 10 Reactions

Not Available

Enzyme 10 Pfam Domain Function

Methyltransf_11 (PF08241 )

Enzyme 10 Signals

None

Enzyme 10 Transmembrane Regions

None

Enzyme 10 Essentiality

Not Available

Enzyme 10 GenBank ID Protein

45946104

Enzyme 10 UniProtKB/Swiss-Prot ID

O60678

Enzyme 10 UniProtKB/Swiss-Prot Entry Name

ANM3_HUMAN Link Image

Enzyme 10 PDB ID

Not Available

Enzyme 10 Cellular Location

Not Available

Enzyme 10 Gene Sequence

>1596 bp

ATGTGCTCGTTAGCGTCAGGCGCTACCGGCGGCCGGGGCGCTGTGGAGAATGAGGAGGAC
CTGCCAGAACTGTCGGACAGCGGGGACGAGGCCGCCTGGGAGGATGAGGACGATGCAGAT
CTCCCCCACGGCAAGCAGCAGACCCCCTGCCTGTTCTGTAACAGGTTATTCACATCTGCT
GAAGAAACATTTTCACACTGTAAGTCTGAGCATCAGTTTAATATTGACAGCATGGTTCAT
AAACATGGACTTGAATTTTATGGATACATTAAGCTAATAAATTTTATTAGACTTAAGAAT
CCTACAGTTGAGTACATGAATTCCATATACAACCCAGTGCCTTGGGAGAAAGAAGAGTAT
TTGAAGCCAGTATTAGAAGATGACCTTTTACTTCAATTTGATGTAGAAGATCTTTATGAA
CCGGTGTCAGTACCCTTCTCATACCCCAATGGACTCAGTGAAAATACATCTGTTGTTGAA
AAATTGAAACATATGGAAGCCAGGGCACTGTCTGCTGAAGCCGCATTGGCCAGAGCACGT
GAGGATCTGCAGAAAATGAAACAATTTGCTCAGGATTTTGTGATGCACACAGATGTCAGA
ACCTGCTCGTCATCTACTAGTGTCATTGCGGACCTCCAGGAGGATGAGGATGGTGTTTAT
TTCAGCTCATACGGGCATTATGGGATACATGAAGAAATGCTAAAGGACAAAATACGAACA
GAAAGCTACCGAGATTTCATATACCAAAATCCACATATCTTCAAAGACAAGGTAGTTTTG
GATGTTGGGTGTGGAACTGGAATTCTCTCTATGTTTGCTGCTAAAGCTGGGGCGAAGAAG
GTTCTTGGAGTTGATCAATCTGAAATACTTTACCAGGCAATGGATATTATAAGACTAAAT
AAACTTGAAGATACTATTACACTAATTAAAGGAAAGATTGAAGAAGTTCATCTTCCTGTA
GAAAAAGTAGATGTTATCATATCTGAGTGGATGGGCTATTTTCTTCTGTTTGAGTCTATG
TTAGATTCTGTCCTTTATGCAAAGAACAAATACTTGGCAAAAGGAGGCTCGGTCTACCCT
GACATTTGCACTATCAGCCTTGTAGCAGTGAGTGATGTGAATAAACATGCTGATAGAATT
GCTTTTTGGGATGATGTCTATGGCTTCAAGATGTCCTGCATGAAGAAAGCAGTTATTCCA
GAAGCTGTTGTGGAAGTTTTAGATCCGAAGACTCTTATTTCAGAACCTTGTGGTATTAAG
CATATAGATTGCCATACGACGTCTATCTCAGATTTGGAATTTTCATCAGATTTTACCCTG
AAAATCACAAGGACATCCATGTGCACGGCAATTGCTGGCTACTTTGATATATATTTTGAG
AAGAATTGCCACAACAGGGTCGTGTTCTCTACGGGCCCTCAGAGCACCAAAACACACTGG
AAACAAACAGTATTTCTACTGGAAAAACCATTTTCAGTTAAAGCAGGTGAAGCCTTGAAA
GGAAAGGTCACAGTTCACAAGAATAAGAAAGATCCACGTTCTCTCACCGTGACCCTCACG
TTGAATAATTCAACTCAAACTTATGGTCTCCAGTGA

Enzyme 10 GenBank Gene ID

BC037544

Enzyme 10 GeneCard ID

PRMT3

Enzyme 10 GenAtlas ID

PRMT3

Enzyme 10 HGNC ID

HGNC:30163 Link Image

Enzyme 10 Chromosome Location

Enzyme 10 Locus

11p15.1

Enzyme 10 SNPs

SNPJam Report Link Image

Enzyme 10 General References

Tang J, Gary JD, Clarke S, Herschman HR: PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J Biol Chem. 1998 Jul 3;273(27):16935-45. [PubMed ]

Enzyme 10 Metabolite References

Not Available

Enzyme 11 [top]

Enzyme 11 ID

13071

Enzyme 11 Name

Aldeyde oxidase

Enzyme 11 Synonyms

Aldehyde oxidase 1, isoform CRA_b
Aldehyde oxidase 1

Enzyme 11 Gene Name

hAO

Enzyme 11 Protein Sequence

>Aldeyde oxidase

MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYN
PITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPG
MVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTSGCCQSKENGVCC
LDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTRVFGSER
MMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHA
YNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHII
SRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSR
KWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKL
IGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPV
HYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYC
DDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAE
KFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPE
RKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKY
IQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGE
DMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKF
PNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAAKCGLSPEKVRIINMYKEID
QTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLGS
RAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETV
PNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVG
YFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAID
IGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSN
TLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFT
KMIPRDEPGSYVPWNVPI

Enzyme 11 Number of Residues

1338

Enzyme 11 Molecular Weight

147920

Enzyme 11 Theoretical pI

7.17

Enzyme 11 GO Classification

Function
binding catalytic activity cation binding electron transporter activity ion binding iron ion binding metal ion binding oxidoreductase activity transition metal ion binding transporter activity
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
—

Enzyme 11 General Function

Nucleotide transport and metabolism

Enzyme 11 Specific Function

Not Available

Enzyme 11 Pathways

Nicotinate and Nicotinamide Metabolism (map00760 )
Tryptophan Metabolism (map00380 )
Tyrosine Metabolism (map00350 )
Valine, Leucine and Isoleucine Degradation (map00280 )
Vitamin B6 Metabolism (map00750 )

Enzyme 11 Reactions

an aldehyde + H2O + O2 = a carboxylic acid + H2O2 [RN:R00635] ALL_REAC R00635 > R02657 R04904
(other) R01709 R02655 R03871 R04085

Enzyme 11 Pfam Domain Function

Ald_Xan_dh_C (PF01315 )
Ald_Xan_dh_C2 (PF02738 )
CO_deh_flav_C (PF03450 )
FAD_binding_5 (PF00941 )
Fer2 (PF00111 )
Fer2_2 (PF01799 )

Enzyme 11 Signals

None

Enzyme 11 Transmembrane Regions

None

Enzyme 11 Essentiality

Not Available

Enzyme 11 GenBank ID Protein

109658814

Enzyme 11 UniProtKB/Swiss-Prot ID

Q9BYF0

Enzyme 11 UniProtKB/Swiss-Prot Entry Name

Q9BYF0_HUMAN Link Image

Enzyme 11 PDB ID

Not Available

Enzyme 11 Cellular Location

Not Available

Enzyme 11 Gene Sequence

Not Available

Enzyme 11 GenBank Gene ID

BC117179

Enzyme 11 GeneCard ID

Q9BYF0

Enzyme 11 GenAtlas ID

hAO

Enzyme 11 HGNC ID

HGNC:553

Enzyme 11 Chromosome Location

Not Available

Enzyme 11 Locus

Not Available

Enzyme 11 SNPs

SNPJam Report Link Image

Enzyme 11 General References

Ichida K, Matsumura T, Sakuma R, Hosoya T, Nishino T: Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II. Biochem Biophys Res Commun. 2001 Apr 20;282(5):1194-200. [PubMed ]
Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed ]

Enzyme 11 Metabolite References

Not Available

Enzyme 12 [top]

Enzyme 12 ID

16425

Enzyme 12 Name

cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a)

Enzyme 12 Synonyms

Not Available

Enzyme 12 Gene Name

MAOB

Enzyme 12 Protein Sequence

>cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a)

MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSY
VGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWR
TMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEV
SALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQ
TRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVY
YKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEER
LKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDR
IYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTT
FLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV

Enzyme 12 Number of Residues

520

Enzyme 12 Molecular Weight

58764

Enzyme 12 Theoretical pI

7.55

Enzyme 12 GO Classification

Function
catalytic activity oxidoreductase activity
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
—

Enzyme 12 General Function

Amino acid transport and metabolism

Enzyme 12 Specific Function

Not Available

Enzyme 12 Pathways

Not Available

Enzyme 12 Reactions

Not Available

Enzyme 12 Pfam Domain Function

Amino_oxidase (PF01593 )

Enzyme 12 Signals

None

Enzyme 12 Transmembrane Regions

None

Enzyme 12 Essentiality

Not Available

Enzyme 12 GenBank ID Protein

Not Available

Enzyme 12 UniProtKB/Swiss-Prot ID

B2R6R3

Enzyme 12 UniProtKB/Swiss-Prot Entry Name

B2R6R3_HUMAN Link Image

Enzyme 12 PDB ID

2BK3

Enzyme 12 PDB File

Show

Enzyme 12 3D Structure

Enzyme 12 Cellular Location

Not Available

Enzyme 12 Gene Sequence

Not Available

Enzyme 12 GenBank Gene ID

AK312679

Enzyme 12 GeneCard ID

B2R6R3

Enzyme 12 GenAtlas ID

Not Available

Enzyme 12 HGNC ID

Not Available

Enzyme 12 Chromosome Location

Not Available

Enzyme 12 Locus

Not Available

Enzyme 12 SNPs

SNPJam Report Link Image

Enzyme 12 General References

Not Available

Enzyme 12 Metabolite References

Not Available

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Human Metabolome Database Version 2.5

Showing metabocard for 5-Hydroxyindoleacetaldehyde (HMDB04073)