| Version |
2.5 |
| Creation Date |
2008-10-16 23:33:06 |
| Update Date |
2009-10-02 16:14:18 |
| Accession Number |
HMDB11118 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Se-Adenosylselenomethionine |
| Description |
Se-Adenosylselenomethionine is an intermediate in Selenoamino acid metabolism. Se-Adenosylselenomethionine is converted from Selenomethionine via the enzyme S-adenosylmethionine synthetase (EC 2.5.1.6). It is then
converted to Se-Adenosylselenohomocysteine via the enzyme Transferases (EC 2.1.1.-). |
| Synonyms |
Not Available |
| Chemical IUPAC Name |
Not Available |
| Chemical Formula |
C15H23N6O5Se |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
| — |
| Class |
| — |
| Sub Class |
| — |
| Family |
|
| Species |
- cation
- secondary alcohol
- 1,2-diol
- primary amine
- primary aliphatic amine (alkylamine)
- primary aromatic amine
- carboxylic acid
- aromatic compound
- heterocyclic compound
- alpha-aminoacid
|
| Biofunction |
| — |
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
446.340 |
| Monoisotopic Molecular Weight |
447.089508 |
| Isomeric SMILES |
C[Se+](CCC(N)C(O)=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC2=C1N=CN=C2N |
| Canonical SMILES |
C[Se+](CCC(N)C(O)=O)CC1OC(C(O)C1O)N1C=NC2=C1N=CN=C2N |
| KEGG Compound ID |
C05691  |
| BioCyc ID |
Not Available |
| BiGG ID |
46296  |
| Wikipedia Link |
Not Available |
| NuGOwiki Link |
HMDB11118  |
| Metagene Link |
HMDB11118  |
| METLIN ID |
Not Available |
| PubChem Compound |
24892761  |
| PubChem Substance |
7998  |
| ChEBI ID |
Not Available |
| CAS Registry Number |
Not Available |
| InChI Identifier |
InChI=1/C15H22N6O5Se/c1-27(3-2-7(16)15(24)25)4-8-10(22)11(23)14(26-8)21-6-20-9-12(17)18-5-19-13(9)21/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25)/p+1/t7?,8-,10-,11-,14-,27?/m1/s1 |
| Synthesis Reference |
Not Available |
| Melting Point (Experimental) |
Not Available |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
1.79 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
1 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
Not Available
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-1.93 [Predicted by ALOGPS]
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 |
Not Available Not Available
|
| Predicted 13C NMR Spectrum |
Not Available Not Available
|
| Mass Spectrum |
Not Available |
| Simplified TOCSY Spectrum |
Not Available |
| BMRB Spectrum |
Not Available |
| Cellular Location |
Not Available |
| 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 |
|
| General References |
Not Available |
| Metabolic Enzymes |
- S-adenosylmethionine synthetase isoform type-1
- Protein arginine N-methyltransferase 3
- Methionine adenosyltransferase 2 subunit beta
- Methionine adenosyltransferase II, beta, isoform CRA_a
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5655 |
| Enzyme 1 Name |
S-adenosylmethionine synthetase isoform type-1 |
| Enzyme 1 Synonyms |
- Methionine adenosyltransferase 1
- AdoMet synthetase 1
- Methionine adenosyltransferase I/III
- MAT-I/III
|
| Enzyme 1 Gene Name |
MAT1A |
| Enzyme 1 Protein Sequence |
>S-adenosylmethionine synthetase isoform type-1
MNGPVDGLCDHSLSEGVFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVC
KTGMVLLCGEITSMAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQC
VHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIILAHKLNARMADLRRSGLLPWLRPDS
KTQVTVQYMQDNGAVIPVRIHTIVISVQHNEDITLEEMRRALKEQVIRAVVPAKYLDEDT
VYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARW
VAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSQKTERELLDVVHKNFDLRPGVI
VRDLDLKKPIYQKTACYGHFGRSEFPWEVPRKLVF
|
| Enzyme 1 Number of Residues |
395 |
| Enzyme 1 Molecular Weight |
43648 |
| Enzyme 1 Theoretical pI |
6.24 |
| Enzyme 1 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- methionine adenosyltransferase activity
- nucleotide binding
- purine nucleotide binding
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- cellular metabolism
- metabolism
- one-carbon compound metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Coenzyme transport and metabolism |
| Enzyme 1 Specific Function |
Catalyzes the formation of S-adenosylmethionine from methionine and ATP |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
220066  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q00266  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
METK1_HUMAN  |
| Enzyme 1 PDB ID |
1O9T  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1188 bp
ATGAATGGACCGGTGGATGGCTTGTGTGACCACTCTCTAAGTGAAGGAGTCTTCATGTTC
ACATCGGAGTCTGTGGGAGAGGGACACCCGGATAAGATCTGTGACCAGATCAGTGATGCA
GTGCTGGATGCCCATCTCAAGCAAGACCCCAATGCCAAGGTGGCCTGTGAGACAGTGTGC
AAGACCGGCATGGTGCTGCTGTGTGGTGAGATCACCTCAATGGCCATGGTGGACTACCAG
CGGGTGGTGAGGGACACCATCAAGCACATCGGCTACGATGACTCAGCCAAGGGCTTTGAC
TTCAAGACTTGCAACGTGCTGGTGGCTTTGGAGCAGCAATCCCCAGATATTGCCCAGTGC
GTCCATCTGGACAGAAATGAGGAGGATGTGGGGGCAGGAGATCAGGGTTTGATGTTCGGC
TATGCCACCGACGAGACAGAGGAGTGCATGCCCCTCACCATCATCCTTGCTCACAAGCTC
AACGCCCGGATGGCAGACCTCAGGCGCTCCGGCCTCCTCCCCTGGCTGCGGCCTGACTCT
AAGACTCAGGTGACAGTTCAGTACATGCAGGACAATGGCGCAGTCATCCCTGTGCGCATC
CACACCATCGTCATCTCTGTGCAGCACAACGAAGACATCACGCTGGAGGAGATGCGCAGG
GCCCTGAAGGAGCAAGTCATCAGGGCCGTGGTGCCGGCCAAGTACCTGGACGAAGACACC
GTCTACCACCTGCAGCCCAGTGGGCGGTTTGTCATCGGAGGTCCCCAGGGGGATGCGGGT
GTCACTGGCCGTAAGATTATTGTGGACACCTATGCGGCCTGGGGGGCTCATGGTGGTGGG
GCCTTCTCTGGGAAGGACTACACCAAGGTGGACCGCTCAGCCGCATATGCTGCCCGCTGG
GTGGCCAAGTCTCTGGTGAAAGCAGGGCTCTGCCGGAGAGTGCTTGTCCAGGTTTCCTAT
GCCATTGGTGTGGCCGAGCCGCTGTCCATTTCCATCTTCACCTACGGAACCTCTCAGAAG
ACAGAGCGAGAGCTGCTGGATGTGGTGCATAAGAACTTCGACCTCCGGCCGGGCGTCATT
GTCAGGGACTTGGATTTGAAGAAGCCCATCTACCAGAAGACAGCATGCTACGGCCATTTC
GGAAGAAGCGAGTTCCCATGGGAGGTTCCCAGGAAGCTTGTATTTTAG
|
| Enzyme 1 GenBank Gene ID |
D49357  |
| Enzyme 1 GeneCard ID |
MAT1A  |
| Enzyme 1 GenAtlas ID |
MAT1A  |
| Enzyme 1 HGNC ID |
HGNC:6903  |
| Enzyme 1 Chromosome Location |
Not Available |
| Enzyme 1 Locus |
Not Available |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Alvarez L, Corrales F, Martin-Duce A, Mato JM: Characterization of a full-length cDNA encoding human liver S-adenosylmethionine synthetase: tissue-specific gene expression and mRNA levels in hepatopathies. Biochem J. 1993 Jul 15;293 ( Pt 2):481-6. [PubMed
]
- Horikawa S, Tsukada K: Molecular cloning and nucleotide sequence of cDNA encoding the human liver S-adenosylmethionine synthetase. Biochem Int. 1991 Sep;25(1):81-90. [PubMed
]
- Ubagai T, Lei KJ, Huang S, Mudd SH, Levy HL, Chou JY: Molecular mechanisms of an inborn error of methionine pathway. Methionine adenosyltransferase deficiency. J Clin Invest. 1995 Oct;96(4):1943-7. [PubMed
]
- Chamberlin ME, Ubagai T, Mudd SH, Wilson WG, Leonard JV, Chou JY: Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency. J Clin Invest. 1996 Aug 15;98(4):1021-7. [PubMed
]
- Chamberlin ME, Ubagai T, Mudd SH, Levy HL, Chou JY: Dominant inheritance of isolated hypermethioninemia is associated with a mutation in the human methionine adenosyltransferase 1A gene. Am J Hum Genet. 1997 Mar;60(3):540-6. [PubMed
]
- Chamberlin ME, Ubagai T, Mudd SH, Thomas J, Pao VY, Nguyen TK, Levy HL, Greene C, Freehauf C, Chou JY: Methionine adenosyltransferase I/III deficiency: novel mutations and clinical variations. Am J Hum Genet. 2000 Feb;66(2):347-55. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5714 |
| Enzyme 2 Name |
Protein arginine N-methyltransferase 3 |
| Enzyme 2 Synonyms |
- Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3
|
| Enzyme 2 Gene Name |
PRMT3 |
| Enzyme 2 Protein Sequence |
>Protein arginine N-methyltransferase 3
MCSLASGATGGRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCLFCNRLFTSA
EETFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWEKEEY
LKPVLEDDLLLQFDVEDLYEPVSVPFSYPNGLSENTSVVEKLKHMEARALSAEAALARAR
EDLQKMKQFAQDFVMHTDVRTCSSSTSVIADLQEDEDGVYFSSYGHYGIHEEMLKDKIRT
ESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVLGVDQSEILYQAMDIIRLN
KLEDTITLIKGKIEEVHLPVEKVDVIISEWMGYFLLFESMLDSVLYAKNKYLAKGGSVYP
DICTISLVAVSDVNKHADRIAFWDDVYGFKMSCMKKAVIPEAVVEVLDPKTLISEPCGIK
HIDCHTTSISDLEFSSDFTLKITRTSMCTAIAGYFDIYFEKNCHNRVVFSTGPQSTKTHW
KQTVFLLEKPFSVKAGEALKGKVTVHKNKKDPRSLTVTLTLNNSTQTYGLQ
|
| Enzyme 2 Number of Residues |
531 |
| Enzyme 2 Molecular Weight |
59904 |
| Enzyme 2 Theoretical pI |
5.00 |
| Enzyme 2 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 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins |
| Enzyme 2 Pathways |
Not Available |
| Enzyme 2 Reactions |
Not Available |
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
45946104  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
O60678  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ANM3_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 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 2 GenBank Gene ID |
BC037544  |
| Enzyme 2 GeneCard ID |
PRMT3  |
| Enzyme 2 GenAtlas ID |
PRMT3  |
| Enzyme 2 HGNC ID |
HGNC:30163  |
| Enzyme 2 Chromosome Location |
11 |
| Enzyme 2 Locus |
11p15.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 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 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
9553 |
| Enzyme 3 Name |
Methionine adenosyltransferase 2 subunit beta |
| Enzyme 3 Synonyms |
- Methionine adenosyltransferase II beta
- MAT II beta
- Methionine adenosyltransferase 2 beta subunit
- DTDP-4-keto-6-deoxy-D-glucose 4- reductase
|
| Enzyme 3 Gene Name |
MAT2B |
| Enzyme 3 Protein Sequence |
>Methionine adenosyltransferase 2 subunit beta
MVGREKELSIHFVPGSCRLVEEEVNIPNRRVLVTGATGLLGRAVHKEFQQNNWHAVGCGF
RRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAASQLNVDASGNL
AKEAAAVGAFLIYISSDYVFDGTNPPYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVL
RIPILYGEVEKLEESAVTVMFDKVQFSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRML
DPSIKGTFHWSGNEQMTKYEMACAIADAFNLPSSHLRPITDSPVLGAQRPRNAQLDCSKL
ETLGIGQRTPFRIGIKESLWPFLIDKRWRQTVFH
|
| Enzyme 3 Number of Residues |
334 |
| Enzyme 3 Molecular Weight |
37552 |
| Enzyme 3 Theoretical pI |
Not Available |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- dTDP-4-dehydrorhamnose reductase activity
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
|
| Process |
- carbohydrate biosynthesis
- extracellular polysaccharide biosynthesis
- macromolecule biosynthesis
- macromolecule metabolism
- metabolism
- physiological process
- polysaccharide biosynthesis
|
| Component |
| — |
|
| Enzyme 3 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 3 Specific Function |
Non-catalytic regulatory subunit of S-adenosylmethionine synthetase 2 (MAT2A), an enzyme that catalyzes the formation of S- adenosylmethionine from methionine and ATP. Regulates the activity of S-adenosylmethionine synthetase 2 by changing its kinetic properties, rendering the enzyme more susceptible to S- adenosylmethionine inhibition |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
- ATP + H2O + L-Methionine --> S-Adenosyl-L-methionine + Phosphate + Diphosphate
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
6815285  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q9NZL9  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
MAT2B_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
Not Available |
| Enzyme 3 GenBank Gene ID |
AF182814  |
| Enzyme 3 GeneCard ID |
Not Available |
| Enzyme 3 GenAtlas ID |
MAT2B  |
| Enzyme 3 HGNC ID |
HGNC:6905  |
| Enzyme 3 Chromosome Location |
Not Available |
| Enzyme 3 Locus |
Not Available |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- LeGros HL Jr, Halim AB, Geller AM, Kotb M: Cloning, expression, and functional characterization of the beta regulatory subunit of human methionine adenosyltransferase (MAT II). J Biol Chem. 2000 Jan 28;275(4):2359-66. [PubMed
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
16535 |
| Enzyme 4 Name |
Methionine adenosyltransferase II, beta, isoform CRA_a |
| Enzyme 4 Synonyms |
- SubName: cDNA, FLJ92687, Homo sapiens methionine adenosyltransferase II, beta (MAT2B), mRNA
|
| Enzyme 4 Gene Name |
MAT2B |
| Enzyme 4 Protein Sequence |
>Methionine adenosyltransferase II, beta, isoform CRA_a
MVGREKELSIHFVPGSCRLVEEEVNIPNRRVLVTGATGLLGRAVHKEFQQNNWHAVGCGF
RRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAASQLNVDASGNL
AKEAAAVGAFLIYISSDYVFDGTNPPYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVL
RIPILYGEVEKLEESAVTVMFDKVQFSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRML
DPSIKGTFHWSGNEQMTKYEMACAIADAFNLPSSHLRPITDSPVLGAQRPRNAQLDCSKL
ETLGIGQRTPFRIGIKESLWPFLIDKRWRQTVFH
|
| Enzyme 4 Number of Residues |
334 |
| Enzyme 4 Molecular Weight |
37552 |
| Enzyme 4 Theoretical pI |
7.39 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- dTDP-4-dehydrorhamnose reductase activity
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
|
| Process |
- carbohydrate biosynthesis
- extracellular polysaccharide biosynthesis
- macromolecule biosynthesis
- macromolecule metabolism
- metabolism
- physiological process
- polysaccharide biosynthesis
|
| Component |
| — |
|
| Enzyme 4 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
Not Available |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
B2R5Y6  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
B2R5Y6_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
Not Available |
| Enzyme 4 GenBank Gene ID |
AK312365  |
| Enzyme 4 GeneCard ID |
B2R5Y6  |
| Enzyme 4 GenAtlas ID |
Not Available |
| Enzyme 4 HGNC ID |
Not Available |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |