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Human Metabolome Database Version 2.5

 

Showing metabocard for D-Glyceraldehyde 3-phosphate (HMDB01112)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:30
Accession Number HMDB01112
Secondary Accession Numbers Not Available
Common Name D-Glyceraldehyde 3-phosphate
Description Glyceraldehyde 3-phosphate (G3P) or triose phosphate is an aldotriose, an important metabolic intermediate in both glycolysis and gluconeogenesis, and in tryptophan biosynthesis. G3P is formed from Fructose-1,6-bisphosphate, Dihydroxyacetone phosphate (DHAP),and 1,3-bisphosphoglycerate, (1,3BPG), and this is how glycerol (as DHAP) enters the glycolytic and gluconeogenesis pathways.
Synonyms
  1. 2-hydroxy-3-(phosphonooxy)-Propanal
  2. 3-Phosphoglyceraldehyde
  3. D-Glyceraldehyde 3-phosphate
  4. D-Glyceraldehyde 3-phosphic acid
  5. D-glyceraldehyde-3-P
  6. DL-Glyceraldehyde 3-phosphate
  7. GAP
  8. Glyceraldehyde-3-phosphate
  9. glyceraldehyde-3-P
  10. glyceraldehyde-P
  11. glyceraldehyde-phosphate
Chemical IUPAC Name (2-hydroxy-3-oxo-propoxy)phosphonic acid
Chemical Formula C3H7O6P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Miscellaneous
Class
  • Acyl Phosphates
Sub Class
  • Glycerophosphates
Family
  • Mammalian Metabolite
Species
  • aldehyde
  • secondary alcohol
  • phosphoric acid ester
Biofunction
  • Component of Fructose and mannose metabolism
  • Component of Inositol metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 170.058
Monoisotopic Molecular Weight 169.998032
Isomeric SMILES OC(COP(O)(O)=O)C=O
Canonical SMILES OC(COP(O)(O)=O)C=O
KEGG Compound ID C00118; C00661 Link Image
BioCyc ID GAP Link Image
BiGG ID 35637 Link Image
Wikipedia Link GAP Link Image
NuGOwiki Link HMDB01112 Link Image
Metagene Link HMDB01112 Link Image
METLIN ID 3294 Link Image
PubChem Compound 729 Link Image
PubChem Substance 679903 Link Image
ChEBI ID 17138 Link Image
CAS Registry Number 142-10-9
InChI Identifier InChI=1/C3H7O6P/c4-1-3(5)2-9-10(6,7)8/h1,3,5H,2H2,(H2,6,7,8)
Synthesis Reference Ballou, Clinton E.; Fischer, Hermann O. L. The synthesis of D-glyceraldehyde 3-phosphate. Journal of the American Chemical Society (1955), 77 3329-31.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1000.0 mg/mL [MEYLAN,WM et al. (1996)]; 20.5 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.69 [Predicted by ALOGPS]; -2.5 [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 1DC4 Link Image
Experimental PDB File Show
Experimental PDB Structure
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 (Predicted from LogP)
Biofluid Location
  • Blood
  • Cellular Cytoplasm
Tissue Location
Tissue References
Fibroblasts —
Kidney —
Muscle —
Concentrations (Normal)
Biofluid Blood
Value 4.8 +/- 1.6 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Cellular Cytoplasm
Value 6.70 (5.70-7.70) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Fructose and Mannose Degradation SMP00064 Link Image map00051 Link Image
Gluconeogenesis SMP00128 Link Image map00010 Link Image
Glycerol Phosphate Shuttle SMP00124 Link Image
Glycolysis SMP00040 Link Image map00010 Link Image
Mitochondrial Electron Transport Chain SMP00355 Link Image map00190 Link Image
Pentose Phosphate Pathway SMP00031 Link Image map00030 Link Image
General References
  1. Modun B, Morrissey J, Williams P: The staphylococcal transferrin receptor: a glycolytic enzyme with novel functions. Trends Microbiol. 2000 May;8(5):231-7. [PubMed Link Image]
  2. Zhang J, Jung K, Lein M, Kristiansen G, Rudolph B, Hauptmann S, Schnorr D, Loening SA, Lichtinghagen R: Differential expression of matrix metalloproteinases and their tissue inhibitors in human primary cultured prostatic cells and malignant prostate cell lines. Prostate. 2002 Jan 1;50(1):38-45. [PubMed Link Image]
  3. Kogler H, Schott P, Toischer K, Milting H, Van PN, Kohlhaas M, Grebe C, Kassner A, Domeier E, Teucher N, Seidler T, Knoll R, Maier LS, El-Banayosy A, Korfer R, Hasenfuss G: Relevance of brain natriuretic peptide in preload-dependent regulation of cardiac sarcoplasmic reticulum Ca2+ ATPase expression. Circulation. 2006 Jun 13;113(23):2724-32. Epub 2006 Jun 5. [PubMed Link Image]
  4. Yang Y, Hou Y, Wang CL, Ji SJ: Renal expression of epidermal growth factor and transforming growth factor-beta1 in children with congenital hydronephrosis. Urology. 2006 Apr;67(4):817-21; discussion 821-2. [PubMed Link Image]
  5. Yamamoto T, Moriwaki Y, Takahashi S, Ohata H, Nakano T, Yamakita J, Higashino K: Effect of glucagon on the xylitol-induced increase in the plasma concentration and urinary excretion of purine bases. Metabolism. 1996 Nov;45(11):1354-9. [PubMed Link Image]
  6. Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
  7. Choei H, Sasaki N, Takeuchi M, Yoshida T, Ukai W, Yamagishi S, Kikuchi S, Saito T: Glyceraldehyde-derived advanced glycation end products in Alzheimer's disease. Acta Neuropathol (Berl). 2004 Sep;108(3):189-93. Epub 2004 Jun 17. [PubMed Link Image]
  8. Harper LV, Hilton AC, Jones AF: RT-PCR for the pseudogene-free amplification of the glyceraldehyde-3-phosphate dehydrogenase gene (gapd). Mol Cell Probes. 2003 Oct;17(5):261-5. [PubMed Link Image]
  9. Wikipedia Link Image
Metabolic Enzymes
  1. Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
  2. Glyceraldehyde-3-phosphate dehydrogenase
  3. Transaldolase
  4. Putative deoxyribose-phosphate aldolase
  5. Fructose-bisphosphate aldolase A
  6. Fructose-bisphosphate aldolase C
  7. Fructose-bisphosphate aldolase B
  8. Triosephosphate isomerase
  9. cDNA FLJ76204, highly similar to Homo sapiens transketolase
  10. Triosephosphate isomerase (EC 5.3.1.1) (Fragment)
  11. Glyceraldehyde 3-phosphate dehydrogenase
  12. Glyceraldehyde 3-phosphate dehydrogenase
  13. Triosephosphate isomerase
Enzyme 1 [top]
Enzyme 1 ID 5962
Enzyme 1 Name Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
Enzyme 1 Synonyms
  1. Spermatogenic glyceraldehyde-3-phosphate dehydrogenase
  2. Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2
  3. GAPDH-2
Enzyme 1 Gene Name GAPDHS
Enzyme 1 Protein Sequence >Glyceraldehyde-3-phosphate dehydrogenase, testis-specific 
MSKRDIVLTNVTVVQLLRQPCPVTRAPPPPEPKAEVEPQPQPEPTPVREEIKPPPPPLPP
HPATPPPKMVSVARELTVGINGFGRIGRLVLRACMEKGVKVVAVNDPFIDPEYMVYMFKY
DSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQIPWRAVGSPYVVESTGVYLSIQAAS
DHISAGAQRVVISAPSPDAPMFVMGVNENDYNPGSMNIVSNASCTTNCLAPLAKVIHERF
GIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKL
TGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLG
DTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSHRVVDLLRYMFSRDK
Enzyme 1 Number of Residues 408
Enzyme 1 Molecular Weight 44502
Enzyme 1 Theoretical pI 8.34
Enzyme 1 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity
  • glyceraldehyde-3-phosphate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 1 General Function Carbohydrate transport and metabolism
Enzyme 1 Specific Function May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility
Enzyme 1 Pathways
Enzyme 1 Reactions
  • D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 3046742 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O14556 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name G3PT_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1227 bp 
ATGTCGAAGCGCGACATCGTCCTCACCAATGTCACCGTTGTCCAGTTGCTGCGACAGCCG
TGCCCGGTGACCAGAGCACCGCCCCCACCTGAGCCTAAGGCTGAAGTAGAGCCCCAGCCA
CAACCAGAGCCCACACCAGTCAGGGAGGAAATAAAGCCACCACCGCCACCACTGCCTCCT
CACCCCGCTACTCCTCCTCCTAAGATGGTGTCTGTGGCCCGGGAGCTGACTGTGGGCATC
AATGGATTTGGACGCATCGGTCGCCTGGTCCTGCGCGCCTGCATGGAGAAGGGTGTTAAG
GTGGTGGCTGTGAATGATCCATTCATTGACCCGGAATACATGGTGTACATGTTTAAGTAT
GACTCCACCCACGGCCGATACAAGGGAAGTGTGGAATTCAGGAATGGACAACTGGTCGTG
GACAACCATGAGATCTCTGTCTACCAGTGCAAAGAGCCCAAACAGATCCCCTGGAGGGCT
GTCGGGAGCCCCTACGTGGTGGAGTCCACAGGCGTGTACCTCTCCATACAGGCAGCTTCG
GACCACATCTCTGCAGGTGCTCAACGTGTGGTCATCTCCGCGCCCTCACCGGATGCACCA
ATGTTCGTCATGGGTGTCAATGAAAATGACTATAACCCTGGCTCCATGAACATTGTGAGC
AACGCGTCCTGCACCACCAACTGTTTGGCTCCCCTCGCCAAAGTCATCCACGAGCGATTT
GGGATCGTGGAAGGGTTGATGACCACAGTCCATTCCTACACGGCCACCCAGAAGACAGTG
GACGGGCCATCAAGGAAGGCCTGGCGAGATGGGCGGGGTGCCCACCAGAACATCATCCCA
GCCTCCACTGGGGCTGCGAAAGCTGTGACCAAAGTCATCCCAGAGCTCAAAGGGAAGCTG
ACAGGGATGGCGTTCCGGGTACCAACCCCGGATGTGTCTGTCGTGGACCTGACCTGCCGC
CTCGCCCAGCCTGCCCCCTACTCAGCCATCAAGGAGGCTGTAAAAGCAGCAGCCAAGGGG
CCCATGGCTGGCATCCTTGCCTACACCGAGGATGAGGTCGTCTCTACGGACTTCCTCGGT
GATACCCACTCGTCCATCTTCGATGCTAAGGCCGGCATTGCGCTCAATGACAATTTCGTG
AAGCTCATTTCATGGTACGACAACGAATATGGCTACAGTCACCGGGTGGTCGACCTCCTC
CGCTACATGTTCAGCCGAGACAAGTGA
Enzyme 1 GenBank Gene ID AJ005371 Link Image
Enzyme 1 GeneCard ID GAPDHS Link Image
Enzyme 1 GenAtlas ID GAPDHS Link Image
Enzyme 1 HGNC ID HGNC:24864 Link Image
Enzyme 1 Chromosome Location 19
Enzyme 1 Locus 19q13.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Welch JE, Brown PL, O'Brien DA, Magyar PL, Bunch DO, Mori C, Eddy EM: Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells. J Androl. 2000 Mar-Apr;21(2):328-38. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5968
Enzyme 2 Name Glyceraldehyde-3-phosphate dehydrogenase
Enzyme 2 Synonyms
  1. GAPDH
Enzyme 2 Gene Name GAPDH
Enzyme 2 Protein Sequence >Glyceraldehyde-3-phosphate dehydrogenase 
MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTV
KAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVI
ISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHA
ITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV
SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAG
IALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE
Enzyme 2 Number of Residues 335
Enzyme 2 Molecular Weight 36054
Enzyme 2 Theoretical pI 8.73
Enzyme 2 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity
  • glyceraldehyde-3-phosphate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 2 General Function Carbohydrate transport and metabolism
Enzyme 2 Specific Function D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH
Enzyme 2 Pathways
Enzyme 2 Reactions
  • D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 31645 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P04406 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name G3P_HUMAN Link Image
Enzyme 2 PDB ID 1J0X Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1008 bp 
ATGGGGAAGGTGAAGGTCGGAGTCAACGGATTTGGTCGTATTGGGCGCCTGGTCACCAGG
GCTGCTTTTAACTCTGGTAAAGTGGATATTGTTGCCATCAATGACCCCTTCATTGACCTC
AACTACATGGTTTACATGTTCCAATATGATTCCACCCATGGCAAATTCCATGGCACCGTC
AAGGCTGAGAACGGGAAGCTTGTCATCAATGGAAATCCCATCACCATCTTCCAGGAGCGA
GATCCCTCCAAAATCAAGTGGGGCGATGCTGGCGCTGAGTACGTCGTGGAGTCCACTGGC
GTCTTCACCACCATGGAGAAGGCTGGGGCTCATTTGCAGGGGGGAGCCAAAAGGGTCATC
ATCTCTGCCCCCTCTGCTGATGCCCCCATGTTCGTCATGGGTGTGAACCATGAGAAGTAT
GACAACAGCCTCAAGATCATCAGCAATGCCTCCTGCACCACCAACTGCTTAGCACCCCTG
GCCAAGGTCATCCATGACAACTTTGGTATCGTGGAAGGACTCATGACCACAGTCCATGCC
ATCACTGCCACCCAGAAGACTGTGGATGGCCCCTCCGGGAAACTGTGGCGTGATGGCCGC
GGGGCTCTCCAGAACATCATCCCTGCCTCTACTGGCGCTGCCAAGGCTGTGGGCAAGGTC
ATCCCTGAGCTAGACGGGAAGCTCACTGGCATGGCCTTCCGTGTCCCCACTGCCAACGTG
TCAGTGGTGGACCTGACCTGCCGTCTAGAAAAACCTGCCAAATATGATGACATCAAGAAG
GTGGTGAAGCAGGCGTCGGAGGGCCCCCTCAAAGGCATCCTGGGCTACACTGAGCACCAG
GTGGTCTCCTCTGACTTCAACAGCGACACCCACTCCTCCACCTTTGACGCTGGGGCTGGC
ATTGCCCTCAACGACCACTTTGTCAAGCTCATTTCCTGGTATGACAACGAATTTGGCTAC
AGCAACAGGGTGGTGGACCTCATGGCCCACATGGCCTCCAAGGAGTAA
Enzyme 2 GenBank Gene ID X01677 Link Image
Enzyme 2 GeneCard ID GAPDH Link Image
Enzyme 2 GenAtlas ID GAPDH Link Image
Enzyme 2 HGNC ID HGNC:4141 Link Image
Enzyme 2 Chromosome Location 12
Enzyme 2 Locus 12p13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Hanauer A, Mandel JL: The glyceraldehyde 3 phosphate dehydrogenase gene family: structure of a human cDNA and of an X chromosome linked pseudogene; amazing complexity of the gene family in mouse. EMBO J. 1984 Nov;3(11):2627-33. [PubMed Link Image]
  2. Arcari P, Martinelli R, Salvatore F: The complete sequence of a full length cDNA for human liver glyceraldehyde-3-phosphate dehydrogenase: evidence for multiple mRNA species. Nucleic Acids Res. 1984 Dec 11;12(23):9179-89. [PubMed Link Image]
  3. Tso JY, Sun XH, Kao TH, Reece KS, Wu R: Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene. Nucleic Acids Res. 1985 Apr 11;13(7):2485-502. [PubMed Link Image]
  4. Tokunaga K, Nakamura Y, Sakata K, Fujimori K, Ohkubo M, Sawada K, Sakiyama S: Enhanced expression of a glyceraldehyde-3-phosphate dehydrogenase gene in human lung cancers. Cancer Res. 1987 Nov 1;47(21):5616-9. [PubMed Link Image]
  5. Allen RW, Trach KA, Hoch JA: Identification of the 37-kDa protein displaying a variable interaction with the erythroid cell membrane as glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem. 1987 Jan 15;262(2):649-53. [PubMed Link Image]
  6. Ercolani L, Florence B, Denaro M, Alexander M: Isolation and complete sequence of a functional human glyceraldehyde-3-phosphate dehydrogenase gene. J Biol Chem. 1988 Oct 25;263(30):15335-41. [PubMed Link Image]
  7. Meyer-Siegler K, Mauro DJ, Seal G, Wurzer J, deRiel JK, Sirover MA: A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8460-4. [PubMed Link Image]
  8. Ye Z, Connor JR: cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs. Biochem Biophys Res Commun. 2000 Aug 18;275(1):223-7. [PubMed Link Image]
  9. Nowak K, Wolny M, Banas T: The complete amino acid sequence of human muscle glyceraldehyde 3-phosphate dehydrogenase. FEBS Lett. 1981 Nov 16;134(2):143-6. [PubMed Link Image]
  10. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  11. Kovalyov LI, Shishkin SS, Efimochkin AS, Kovalyova MA, Ershova ES, Egorov TA, Musalyamov AK: The major protein expression profile and two-dimensional protein database of human heart. Electrophoresis. 1995 Jul;16(7):1160-9. [PubMed Link Image]
  12. Nowak K, Kuczek M, Ostropolska L, Malarska A, Wolny M, Baranowski T: The covalent structure of glyceraldehyde-phosphate dehydrogenase from human muscles. Isolation and amino acid sequences of peptides from tryptic digest. Hoppe Seylers Z Physiol Chem. 1975 Jul;356(7):1181-3. [PubMed Link Image]
  13. Mercer WD, Winn SI, Watson HC: Twinning in crystals of human skeletal muscle D-glyceraldehyde-3-phosphate dehydrogenase. J Mol Biol. 1976 Jun 14;104(1):277-83. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6082
Enzyme 3 Name Transaldolase
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name TALDO1
Enzyme 3 Protein Sequence >Transaldolase 
MSSSPVKRQRMESALDQLKQFTTVVADTGDFHAIDEYKPQDATTNPSLILAAAQMPAYQE
LVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVA
RARRLIELYKEAGISKDRILIKLSSTWEGIQAGKELEEQHGIHCNMTLLFSFAQAVACAE
AGVTLISPFVGRILDWHVANTDKKSYEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRN
TGEIKALAGCDFLTISPKLLGELLQDNAKLVPVLSAKAAQASDLEKIHLDEKSFRWLHNE
DQMAVEKLSDGIRKFAADAVKLERMLTERMFNAENGK
Enzyme 3 Number of Residues 337
Enzyme 3 Molecular Weight 37540
Enzyme 3 Theoretical pI 6.80
Enzyme 3 GO Classification
Function
  • catalytic activity
  • transaldolase activity
  • transferase activity
  • transferase activity, transferring aldehyde or ketonic groups
Process
  • alcohol metabolism
  • carbohydrate metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • hexose metabolism
  • macromolecule metabolism
  • metabolism
  • monosaccharide metabolism
  • pentose-phosphate shunt
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 3 General Function Carbohydrate transport and metabolism
Enzyme 3 Specific Function Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway
Enzyme 3 Pathways
Enzyme 3 Reactions
  • sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 2073541 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P37837 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name TALDO_HUMAN Link Image
Enzyme 3 PDB ID 1F05 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1014 bp 
ATGTCGAGCTCACCCGTGAAGCGTCAGAGGATGGAGTCCGCGCTGGACCAGCTCAAGCAG
TTCACCACCGTGGTGGCCGACACGGGCGACTTCCACGCCATCGACGAGTACAAGCCCCAG
GATGCTACCACCAACCCGTCCCTGATCCTGGCCGCAGCACAGATGCCCGCTTACCAGGAG
CTGGTGGAGGAGGCGATTGCCTATGGCCGGAAGCTGGGCGGGTCACAAGAGGACCAGATT
AAAAATGCTATTGATAAACTTTTTGTGTTGTTTGGAGCAGAAATACTAAAGAAGATTCCG
GGCCGAGTATCCACAGAAGTAGACGCAAGGCTCTCCTTTGATAAAGATGCGATGGTGGCC
AGAGCCAGGCGGCTCATCGAGCTCTACAAGGAAGCTGGGATCAGCAAGGACCGAATTCTT
ATAAAGCTGTCATCAACCTGGGAAGGAATTCAGGCTGGAAAGGAGCTCGAGGAGCAGCAC
GGCATCCACTGCAACATGACGTTACTCTTCTCCTTCGCCCAGGCTGTGGCCTGTGCCGAG
GCGGGTGTGACCCTCATCTCCCCATTTGTTGGGCGCATCCTTGATTGGCATGTGGCAAAC
ACCGACAAGAAATCCTATGAGCCCCTGGAAGACCCTGGGGTAAAGAGTGTCACTAAAATC
TACAACTACTACAAGAAGTTTAGCTACAAAACCATTGTCATGGGCGCCTCCTTCCGCAAC
ACGGGCGAGATCAAAGCACTGGCCGGCTGTGACTTCCTCACCATCTCACCCAAGCTCCTG
GGAGAGCTGCTGCAGGACAACGCCAAGCTGGTGCCTGTGCTCTCAGCCAAGGCGGCCCAA
GCCAGTGACCTGGAAAAAATCCACCTGGATGAGAAGTCTTTCCGTTGGTTGCACAACGAG
GACCAGATGGCTGTGGAGAAGCTCTCTGACGGGATCCGCAAGTTTGCCGCTGATGCAGTG
AAGCTGGAGCGGATGCTGACAGAACGAATGTTCAATGCAGAGAATGGAAAGTAG
Enzyme 3 GenBank Gene ID L19437 Link Image
Enzyme 3 GeneCard ID TALDO1 Link Image
Enzyme 3 GenAtlas ID TALDO1 Link Image
Enzyme 3 HGNC ID HGNC:11559 Link Image
Enzyme 3 Chromosome Location 11
Enzyme 3 Locus 11p15.5-p15.4
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Banki K, Halladay D, Perl A: Cloning and expression of the human gene for transaldolase. A novel highly repetitive element constitutes an integral part of the coding sequence. J Biol Chem. 1994 Jan 28;269(4):2847-51. [PubMed Link Image]
  2. Banki K, Eddy RL, Shows TB, Halladay DL, Bullrich F, Croce CM, Jurecic V, Baldini A, Perl A: The human transaldolase gene (TALDO1) is located on chromosome 11 at p15.4-p15.5. Genomics. 1997 Oct 1;45(1):233-8. [PubMed Link Image]
  3. Kusuda J, Hirai M, Toyoda A, Tanuma R, Nomura-Kitabayashi A, Hashimoto K: Cloning and chromosomal localization of a paralog and a mouse homolog of the human transaldolase gene. Gene. 1998 Mar 16;209(1-2):13-21. [PubMed Link Image]
  4. Perl A, Colombo E, Samoilova E, Butler MC, Banki K: Human transaldolase-associated repetitive elements are transcribed by RNA polymerase III. J Biol Chem. 2000 Mar 10;275(10):7261-72. [PubMed Link Image]
  5. Verhoeven NM, Huck JH, Roos B, Struys EA, Salomons GS, Douwes AC, van der Knaap MS, Jakobs C: Transaldolase deficiency: liver cirrhosis associated with a new inborn error in the pentose phosphate pathway. Am J Hum Genet. 2001 May;68(5):1086-92. Epub 2001 Mar 27. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6233
Enzyme 4 Name Putative deoxyribose-phosphate aldolase
Enzyme 4 Synonyms
  1. Phosphodeoxyriboaldolase
  2. Deoxyriboaldolase
  3. DERA
Enzyme 4 Gene Name DERA
Enzyme 4 Protein Sequence >Putative deoxyribose-phosphate aldolase 
MSAHNRGTELDLSWISKIQVNHPAVLRRAEQIQARRTVKKEWQAAWLLKAVTFIDLTTLS
GDDTSSNIQRLCYKAKYPIREDLLKALNMHDKGITTAAVCVYPARVCDAVKALKAAGCNI
PVASVAAGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWEALYDEIRQFRK
ACGEAHLKTILATGELGTLTNVYKASMIAMMAGSDFIKTSTGKETVNATFPVAIVMLRAI
RDFFWKTGNKIGFKPAGGIRSAKDSLAWLSLVKEELGDEWLKPELFRIGASTLLSDIERQ
IYHHVTGRYAAYHDLPMS
Enzyme 4 Number of Residues 318
Enzyme 4 Molecular Weight 35231
Enzyme 4 Theoretical pI 9.31
Enzyme 4 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • deoxyribose-phosphate aldolase activity
  • lyase activity
Process
  • cellular metabolism
  • deoxyribonucleotide catabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide catabolism
  • nucleotide metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 4 General Function Nucleotide transport and metabolism
Enzyme 4 Specific Function 2-deoxy-D-ribose 5-phosphate = D- glyceraldehyde 3-phosphate + acetaldehyde
Enzyme 4 Pathways
Enzyme 4 Reactions
  • 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 4680691 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9Y315 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name DEOC_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1011 bp 
ATGGTAACAGCTTTCAGGAGCCTACCACGCGGCAGCTCCGGAGCTGCCGCGTCCATGTCC
GCGCACAATCGGGGCACCGAGCTCGACCTTAGCTGGATCTCCAAAATACAAGTGAATCAC
CCGGCAGTTCTGAGGCGTGCGGAACAAATCCAGGCTCGCAGAACCGTGAAAAAGGAGTGG
CAGGCTGCTTGGCTCCTGAAAGCTGTTACCTTTATAGATCTTACTACACTTTCAGGTGAT
GATACATCTTCCAACATTCAAAGGCTCTGTTATAAAGCCAAATACCCAATCCGGGAAGAT
CTCTTAAAAGCTTTAAATATGCATGATAAAGGCATTACTACAGCCGCCGTTTGTGTTTAT
CCCGCCCGGGTGTGTGATGCTGTAAAAGCACTCAAGGCTGCAGGCTGTAATATCCCTGTG
GCATCAGTGGCCGCTGGATTTCCAGCTGGACAGACTCATTTGAAGACACGATTAGAAGAG
ATCAGATTGGCTGTGGAAGATGGAGCTACAGAAATCGACGTGGTAATTAACAGAAGCTTG
GTGCTGACAGGCCAGTGGGAAGCCCTGTATGATGAGATTCGTCAGTTTCGCAAGGCCTGT
GGGGAGGCTCATCTTAAAACTATATTAGCGACAGGAGAACTTGGAACTCTTACTAATGTC
TATAAAGCCAGTATGATAGCAATGATGGCAGGATCAGATTTTATTAAGACCTCTACTGGA
AAAGAAACAGTAAATGCCACCTTCCCGGTAGCTATAGTAATGCTGCGGGCCATTAGAGAT
TTCTTCTGGAAAACTGGAAACAAGATAGGGTTTAAACCAGCAGGAGGCATCCGCAGTGCA
AAGGATTCCCTTGCTTGGCTCTCTCTTGTAAAGGAGGAGCTTGGAGATGAGTGGCTGAAG
CCAGAACTCTTTCGAATAGGTGCCAGTACTCTGCTCTCGGACATTGAGAGGCAGATTTAC
CATCATGTGACTGGAAGATATGCAGCTTATCATGATCTTCCAATGTCTTAA
Enzyme 4 GenBank Gene ID AF132960 Link Image
Enzyme 4 GeneCard ID DERA Link Image
Enzyme 4 GenAtlas ID DERA Link Image
Enzyme 4 HGNC ID HGNC:24269 Link Image
Enzyme 4 Chromosome Location 12
Enzyme 4 Locus 12p12.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6266
Enzyme 5 Name Fructose-bisphosphate aldolase A
Enzyme 5 Synonyms
  1. Muscle-type aldolase
  2. Lung cancer antigen NY-LU-1
Enzyme 5 Gene Name ALDOA
Enzyme 5 Protein Sequence >Fructose-bisphosphate aldolase A 
MPYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYR
QLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTN
GETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQ
NGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHAC
TQKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTF
SYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFVS
NHAY
Enzyme 5 Number of Residues 364
Enzyme 5 Molecular Weight 39420
Enzyme 5 Theoretical pI 8.20
Enzyme 5 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • fructose-bisphosphate aldolase activity
  • lyase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 5 General Function Carbohydrate transport and metabolism
Enzyme 5 Specific Function D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Enzyme 5 Pathways
Enzyme 5 Reactions
  • D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 178351 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P04075 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name ALDOA_HUMAN Link Image
Enzyme 5 PDB ID 4ALD Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1095 bp 
ATGCCCTACCAATATCCAGCACTGACCCCGGAGCAGAAGAAGGAGCTGTCTGACATCGCT
CACCGCATCGTGGCACCTGGCAAGGGCATCCTGGCTGCAGATGAGTCCACTGGGAGCATT
GCCAAGCGGCTGCAGTCCATTGGCACCGAGAACACCGAGGAGAACCGGCGCTTCTACCGC
CAGCTGCTGCTGACAGCTGACGACCGCGTGAACCCCTGCATTGGGGGTGTCATCCTCTTC
CATGAGACACTCTACCAGAAGGCGGATGATGGGCGTCCCTTCCCCCAAGTTATCAAATCC
AAGGGCGGTGTTGTGGGCATCAAGGTAGACAAGGGCGTGGTCCCCCTGGCAGGGACAAAT
GGCGAGACTACCACCCAAGGGTTGGATGGGCTGTCTGAGCGCTGTGCCCAGTACAAGAAG
GACGGAGCTGACTTCGCCAAGTGGCGTTGTGTGCTGAAGATTGGGGAACACACCCCCTCA
GCCCTCGCCATCATGGAAAATGCCAATGTTCTGGCCCGTTATGCCAGTATCTGCCAGCAG
AATGGCATTGTGCCCATCGTGGAGCCTGAGATCCTCCCTGATGGGGACCATGACTTGAAG
CGCTGCCAGTATGTGACCGAGAAGGTGCTGGCTGCTGTCTACAAGGCTCTGAGTGACCAC
CACATCTACCTGGAAGGCACCTTGCTGAAGCCCAACATGGTCACCCCAGGCCATGCTTGC
ACTCAGAAGTTTTCTCATGAGGAGATTGCCATGGCGACCGTCACAGCGCTGCGCCGCACA
GTGCCCCCCGCTGTCACTGGGATCACCTTCCTGTCTGGAGGCCAGAGTGAGGAGGAGGCG
TCCATCAACCTCAATGCCATTAACAAGTGCCCCCTGCTGAAGCCCTGGGCCCTGACCTTC
TCCTACGGCCGAGCCCTGCAGGCCTCTGCCCTGAAGGCCTGGGGCGGGAAGAAGGAGAAC
CTGAAGGCTGCGCAGGAGGAGTATGTCAAGCGAGCCCTGGCCAACAGCCTTGCCTGTCAA
GGAAAGTACACTCCGAGCGGTCAGGCTGGGGCTGCTGCCAGCGAGTCCCTCTTCGTCTCT
AACCACGCCTATTAA
Enzyme 5 GenBank Gene ID M11560 Link Image
Enzyme 5 GeneCard ID ALDOA Link Image
Enzyme 5 GenAtlas ID ALDOA Link Image
Enzyme 5 HGNC ID HGNC:414 Link Image
Enzyme 5 Chromosome Location 16
Enzyme 5 Locus 16q22-q24
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Sakakibara M, Mukai T, Hori K: Nucleotide sequence of a cDNA clone for human aldolase: a messenger RNA in the liver. Biochem Biophys Res Commun. 1985 Aug 30;131(1):413-20. [PubMed Link Image]
  2. Izzo P, Costanzo P, Lupo A, Rippa E, Borghese AM, Paolella G, Salvatore F: A new human species of aldolase A mRNA from fibroblasts. Eur J Biochem. 1987 Apr 1;164(1):9-13. [PubMed Link Image]
  3. Izzo P, Costanzo P, Lupo A, Rippa E, Paolella G, Salvatore F: Human aldolase A gene. Structural organization and tissue-specific expression by multiple promoters and alternate mRNA processing. Eur J Biochem. 1988 Jul 1;174(4):569-78. [PubMed Link Image]
  4. Mukai T, Arai Y, Yatsuki H, Joh K, Hori K: An additional promoter functions in the human aldolase A gene, but not in rat. Eur J Biochem. 1991 Feb 14;195(3):781-7. [PubMed Link Image]
  5. Freemont PS, Dunbar B, Fothergill-Gilmore LA: The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase. Biochem J. 1988 Feb 1;249(3):779-88. [PubMed Link Image]
  6. Freemont PS, Dunbar B, Fothergill LA: Human skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and o-iodosobenzoic acid-cleavage fragments. Arch Biochem Biophys. 1984 Jan;228(1):342-52. [PubMed Link Image]
  7. Maire P, Gautron S, Hakim V, Gregori C, Mennecier F, Kahn A: Characterization of three optional promoters in the 5' region of the human aldolase A gene. J Mol Biol. 1987 Oct 5;197(3):425-38. [PubMed Link Image]
  8. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  9. Tolan DR, Niclas J, Bruce BD, Lebo RV: Evolutionary implications of the human aldolase-A, -B, -C, and -pseudogene chromosome locations. Am J Hum Genet. 1987 Nov;41(5):907-24. [PubMed Link Image]
  10. Gamblin SJ, Cooper B, Millar JR, Davies GJ, Littlechild JA, Watson HC: The crystal structure of human muscle aldolase at 3.0 A resolution. FEBS Lett. 1990 Mar 26;262(2):282-6. [PubMed Link Image]
  11. Gamblin SJ, Davies GJ, Grimes JM, Jackson RM, Littlechild JA, Watson HC: Activity and specificity of human aldolases. J Mol Biol. 1991 Jun 20;219(4):573-6. [PubMed Link Image]
  12. Dalby A, Dauter Z, Littlechild JA: Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications. Protein Sci. 1999 Feb;8(2):291-7. [PubMed Link Image]
  13. Kishi H, Mukai T, Hirono A, Fujii H, Miwa S, Hori K: Human aldolase A deficiency associated with a hemolytic anemia: thermolabile aldolase due to a single base mutation. Proc Natl Acad Sci U S A. 1987 Dec;84(23):8623-7. [PubMed Link Image]
  14. Takasaki Y, Takahashi I, Mukai T, Hori K: Human aldolase A of a hemolytic anemia patient with Asp-128----Gly substitution: characteristics of an enzyme generated in E. coli transfected with the expression plasmid pHAAD128G. J Biochem (Tokyo). 1990 Aug;108(2):153-7. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6267
Enzyme 6 Name Fructose-bisphosphate aldolase C
Enzyme 6 Synonyms
  1. Brain-type aldolase
Enzyme 6 Gene Name ALDOC
Enzyme 6 Protein Sequence >Fructose-bisphosphate aldolase C 
MPHSYPALSAEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYR
QVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGIVVGIKVDKGVVPLAGTD
GETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISERTPSALAILENANVLARYASICQQ
NGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHAC
PIKYTPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASFNLNAINRCPLPRPWALTF
SYGRALQASALNAWRGQRDNAGAATEEFIKRAEVNGLAAQGKYEGSGEDGGAAAQSLYIA
NHAY
Enzyme 6 Number of Residues 364
Enzyme 6 Molecular Weight 39456
Enzyme 6 Theoretical pI 6.86
Enzyme 6 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • fructose-bisphosphate aldolase activity
  • lyase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 6 General Function Carbohydrate transport and metabolism
Enzyme 6 Specific Function D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Enzyme 6 Pathways
Enzyme 6 Reactions
  • D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 28599 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P09972 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ALDOC_HUMAN Link Image
Enzyme 6 PDB ID 1XFB Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1095 bp 
ATGCCTCACTCGTACCCAGCCCTTTCTGCTGAGCAGAAGAAGGAGTTGTCTGACATTGCC
CTGCGGATTGTAGCCCCGGGCAAAGGCATTCTGGCTGCGGATGAGTCTGTAGGCAGCATG
GCCAAGCGGCTGAGCCAAATTGGGGTGGAAAACACAGAGGAGAACCGCCGGCTGTACCGC
CAGGTCCTGTTCAGTGCTGATGACCGTGTGAAAAAGTGCATTGGAGGCGTCATTTTCTTC
CATGAGACCCTCTACCAGAAAGATGATAATGGTGTTCCCTTCGTCCGAACCATCCAGGAT
AAGGGCATCGTCGTGGGCATCAAGGTTGACAAGGGTGTGGTGCCTCTAGCTGGGACTGAT
GGAGAAACCACCACTCAAGGGCTGGATGGGCTCTCAGAACGCTGTGCCCAATACAAGAAG
GATGGTGCTGACTTTGCCAAGTGGCGCTGTGTGCTGAAAATCAGTGAGCGTACACCCTCT
GCACTTGCCATTCTGGAGAACGCCAACGTGCTGGCCCGTTATGCCAGTATCTGCCAGCAG
AATGGCATTGTGCCTATTGTGGAACCTGAAATATTGCCTGATGGAGACCACGACCTCAAA
CGTTGTCAGTATGTTACAGAGAAGGTCTTGGCTGCTGTGTACAAGGCCCTGAGTGACCAT
CATGTATACCTGGAGGGGACCCTGCTCAAGCCCAACATGGTGACCCCGGGCCATGCCTGT
CCCATCAAGTATACCCCAGAGGAGATTGCCATGGCAACTGTCACTGCCCTGCGTCGCACT
GTGCCCCCAGCTGTCCCAGGAGTGACCTTCCTGTCTGGGGGTCAGAGCGAAGAAGAGGCA
TCATTCAACCTCAATGCCATCAACCGCTGCCCCCTTCCCCGACCCTGGGCGCTTACCTTC
TCCTATGGGCGTGCCCTGCAAGCCTCTGCACTCAATGCCTGGCGAGGGCAACGGGACAAT
GCTGGGGCTGCCACTGAGGAGTTCATCAAGCGGGCTGAGGTGAATGGGCTTGCAGCCCAG
GGCAAGTATGAAGGCAGTGGAGAAGATGGTGGAGCAGCAGCACAGTCACTCTACATTGCC
AACCATGCCTACTGA
Enzyme 6 GenBank Gene ID X05196 Link Image
Enzyme 6 GeneCard ID ALDOC Link Image
Enzyme 6 GenAtlas ID ALDOC Link Image
Enzyme 6 HGNC ID HGNC:418 Link Image
Enzyme 6 Chromosome Location 17
Enzyme 6 Locus 17cen-q12
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Rottmann WH, Deselms KR, Niclas J, Camerato T, Holman PS, Green CJ, Tolan DR: The complete amino acid sequence of the human aldolase C isozyme derived from genomic clones. Biochimie. 1987 Feb;69(2):137-45. [PubMed Link Image]
  2. Buono P, Paolella G, Mancini FP, Izzo P, Salvatore F: The complete nucleotide sequence of the gene coding for the human aldolase C. Nucleic Acids Res. 1988 May 25;16(10):4733. [PubMed Link Image]
  3. Buono P, Mancini FP, Izzo P, Salvatore F: Characterization of the transcription-initiation site and of the promoter region within the 5' flanking region of the human aldolase C gene. Eur J Biochem. 1990 Sep 24;192(3):805-11. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6268
Enzyme 7 Name Fructose-bisphosphate aldolase B
Enzyme 7 Synonyms
  1. Liver-type aldolase
Enzyme 7 Gene Name ALDOB
Enzyme 7 Protein Sequence >Fructose-bisphosphate aldolase B 
MAHRFPALTQEQKKELSEIAQSIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFR
EILFSVDSSINQSIGGVILFHETLYQKDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTN
KETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQ
NGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHAC
TKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSF
SYGRALQASALAAWGGKAANKEATQEAFMKRAMANCQAAKGQYVHTGSSGAASTQSLFTA
CYTY
Enzyme 7 Number of Residues 364
Enzyme 7 Molecular Weight 39473
Enzyme 7 Theoretical pI 7.96
Enzyme 7 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • fructose-bisphosphate aldolase activity
  • lyase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 7 General Function Carbohydrate transport and metabolism
Enzyme 7 Specific Function D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Enzyme 7 Pathways
Enzyme 7 Reactions
  • D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 28617 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P05062 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name ALDOB_HUMAN Link Image
Enzyme 7 PDB ID 1QO5 Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1095 bp 
ATGGCCCACCGATTTCCAGCCCTCACCCAGGAGCAGAAGAAGGAGCTCTCAGAAATTGCC
CAGAGCATTGTTGCCAATGGAAAGGGGATCCTGGCTGCAGATGAATCTGTAGGTACCATG
GGGAACCGCCTGCAGAGGATCAAGGTGGAAAACACTGAAGAGAACCGCCGGCAGTTCCGA
GAAATCCTCTTCTCTGTGGACAGTTCCATCAACCAGAGCATCGGGGGTGTGATCCTTTTC
CACGAGACCCTCTACCAGAAGGACAGCCAGGGAAAGCTGTTCAGAAACATCCTCAAGGAA
AAGGGGATCGTGGTGGGAATCAAGTTAGACCAAGGAGGTGCTCCTCTTGCAGGAACAAAC
AAAGAAACCACCATTCAAGGGCTTGATGGCCTCTCAGAGCGCTGTGCTCAGTACAAGAAA
GATGGTGTTGACTTTGGGAAGTGGCGTGCTGTGCTGAGGATTGCCGACCAGTGTCCATCC
AGCCTCGCTATCCAGGAAAACGCCAACGCCCTGGCTCGCTACGCCAGCATCTGTCAGCAG
AATGGACTGGTACCTATTGTTGAACCAGAGGTAATTCCTGATGGAGACCATGACCTGGAA
CACTGCCAGTATGTTACTGAGAAGGTCCTGGCTGCTGTCTACAAGGCCCTGAATGACCAT
CATGTTTACCTGGAGGGCACCCTGCTAAAGCCCAACATGGTGACTGCTGGACATGCCTGC
ACCAAGAAGTATACTCCAGAACAAGTAGCTATGGCCACCGTAACAGCTCTCCACCGTACT
GTTCCTGCAGCTGTTCCTGGCATCTGCTTTTTGTCTGGTGGCATGAGTGAAGAGGATGCC
ACTCTCAACCTCAATGCTATCAACCTTTGCCCTCTACCAAAGCCCTGGAAACTAAGTTTC
TCTTATGGACGGGCCCTGCAGGCCAGTGCACTGGCTGCCTGGGGTGGCAAGGCTGCAAAC
AAGGAGGCAACCCAGGAGGCTTTTATGAAGCGGGCCATGGCTAACTGCCAGGCGGCCAAA
GGACAGTATGTTCACACGGGTTCTTCTGGGGCTGCTTCCACCCAGTCGCTCTTCACAGCC
TGCTATACCTACTAG
Enzyme 7 GenBank Gene ID X02747 Link Image
Enzyme 7 GeneCard ID ALDOB Link Image
Enzyme 7 GenAtlas ID ALDOB Link Image
Enzyme 7 HGNC ID HGNC:417 Link Image
Enzyme 7 Chromosome Location 9
Enzyme 7 Locus 9q21.3-q22.2
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Paolella G, Santamaria R, Izzo P, Costanzo P, Salvatore F: Isolation and nucleotide sequence of a full-length cDNA coding for aldolase B from human liver. Nucleic Acids Res. 1984 Oct 11;12(19):7401-10. [PubMed Link Image]
  2. Sakakibara M, Mukai T, Yatsuki H, Hori K: Human aldolase isozyme gene: the structure of multispecies aldolase B mRNAs. Nucleic Acids Res. 1985 Jul 25;13(14):5055-69. [PubMed Link Image]
  3. Rottmann WH, Tolan DR, Penhoet EE: Complete amino acid sequence for human aldolase B derived from cDNA and genomic clones. Proc Natl Acad Sci U S A. 1984 May;81(9):2738-42. [PubMed Link Image]
  4. Mukai T, Yatsuki H, Arai Y, Joh K, Matsuhashi S, Hori K: Human aldolase B gene: characterization of the genomic aldolase B gene and analysis of sequences required for multiple polyadenylations. J Biochem (Tokyo). 1987 Nov;102(5):1043-51. [PubMed Link Image]
  5. Tolan DR, Penhoet EE: Characterization of the human aldolase B gene. Mol Biol Med. 1986 Jun;3(3):245-64. [PubMed Link Image]
  6. Sakakibara M, Takahashi I, Takasaki Y, Mukai T, Hori K: Construction and expression of human aldolase A and B expression plasmids in Escherichia coli host. Biochim Biophys Acta. 1989 Apr 12;1007(3):334-42. [PubMed Link Image]
  7. Besmond C, Dreyfus JC, Gregori C, Frain M, Zakin MM, Sala Trepat J, Kahn A: Nucleotide sequence of a cDNA clone for human aldolase B. Biochem Biophys Res Commun. 1983 Dec 16;117(2):601-9. [PubMed Link Image]
  8. Dalby AR, Tolan DR, Littlechild JA: The structure of human liver fructose-1,6-bisphosphate aldolase. Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1526-33. Epub 2001 Oct 25. [PubMed Link Image]
  9. Tolan DR: Molecular basis of hereditary fructose intolerance: mutations and polymorphisms in the human aldolase B gene. Hum Mutat. 1995;6(3):210-8. [PubMed Link Image]
  10. Cross NC, Tolan DR, Cox TM: Catalytic deficiency of human aldolase B in hereditary fructose intolerance caused by a common missense mutation. Cell. 1988 Jun 17;53(6):881-5. [PubMed Link Image]
  11. Cross NC, de Franchis R, Sebastio G, Dazzo C, Tolan DR, Gregori C, Odievre M, Vidailhet M, Romano V, Mascali G, et al.: Molecular analysis of aldolase B genes in hereditary fructose intolerance. Lancet. 1990 Feb 10;335(8685):306-9. [PubMed Link Image]
  12. Brooks CC, Tolan DR: A partially active mutant aldolase B from a patient with hereditary fructose intolerance. FASEB J. 1994 Jan;8(1):107-13. [PubMed Link Image]
  13. Ali M, Cox TM: Diverse mutations in the aldolase B gene that underlie the prevalence of hereditary fructose intolerance. Am J Hum Genet. 1995 Apr;56(4):1002-5. [PubMed Link Image]
  14. Ali M, Sebastio G, Cox TM: Identification of a novel mutation (Leu 256-->Pro) in the human aldolase B gene associated with hereditary fructose intolerance. Hum Mol Genet. 1994 Jan;3(1):203-4. [PubMed Link Image]
  15. Cross NC, Stojanov LM, Cox TM: A new aldolase B variant, N334K, is a common cause of hereditary fructose intolerance in Yugoslavia. Nucleic Acids Res. 1990 Apr 11;18(7):1925. [PubMed Link Image]
  16. Lau J, Tolan DR: Screening for hereditary fructose intolerance mutations by reverse dot-blot. Mol Cell Probes. 1999 Feb;13(1):35-40. [PubMed Link Image]
  17. Santamaria R, Esposito G, Vitagliano L, Race V, Paglionico I, Zancan L, Zagari A, Salvatore F: Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at arginine 303 in human liver aldolase. Biochem J. 2000 Sep 15;350 Pt 3:823-8. [PubMed Link Image]
  18. Sanchez-Gutierrez JC, Benlloch T, Leal MA, Samper B, Garcia-Ripoll I, Feliu JE: Molecular analysis of the aldolase B gene in patients with hereditary fructose intolerance from Spain. J Med Genet. 2002 Sep;39(9):e56. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6880
Enzyme 8 Name Triosephosphate isomerase
Enzyme 8 Synonyms
  1. TIM
  2. Triose-phosphate isomerase
Enzyme 8 Gene Name TPI1
Enzyme 8 Protein Sequence >Triosephosphate isomerase 
MAPSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKI
AVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAE
GLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQ
QAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE
FVDIINAKQ
Enzyme 8 Number of Residues 249
Enzyme 8 Molecular Weight 26670
Enzyme 8 Theoretical pI 6.91
Enzyme 8 GO Classification
Function
  • catalytic activity
  • intramolecular oxidoreductase activity
  • intramolecular oxidoreductase activity, interconverting aldoses and ketoses
  • isomerase activity
  • triose-phosphate isomerase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 8 General Function Carbohydrate transport and metabolism
Enzyme 8 Specific Function D-glyceraldehyde 3-phosphate = glycerone phosphate
Enzyme 8 Pathways
Enzyme 8 Reactions
  • D-glyceraldehyde 3-phosphate = glycerone phosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 339841 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P60174 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name TPIS_HUMAN Link Image
Enzyme 8 PDB ID 1HTI Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >750 bp 
ATGGCGCCCTCCAGGAAGTTCTTCGTTGGGGGAAACTGGAAGATGAACGGGCGGAAGCAG
AGTCTGGGGGAGCTCATCGGCACTCTGAACGCGGCCAAGGTGCCGGCCGACACCGAGGTG
GTTTGTGCTCCCCCTACTGCCTATATCGACTTCGCCCGGCAGAAGCTAGATCCCAAGATT
GCTGTGGCTGCGCAGAACTGCTACAAAGTGACTAATGGGGCTTTTACTGGGGAGATCAGC
CCTGGCATGATCAAAGACTGCGGAGCCACGTGGGTGGTCCTGGGACACTCAGAGAGAAGG
CATGTCTTTGGGGAGTCAGATGAGCTGATTGGGCAGAAAGTGGCCCATGCTCTGGCAGAG
GGACTCGGAGTAATCGCCTGCATTGGGGAGAAGCTAGATGAAAGGGAAGCTGGCATCACT
GAGAAGGTTGTTTTCGAGCAGACAAAGGTCATCGCAGATAACGTGAAGGACTGGAGCAAG
GTCGTCCTCGCCTATGAGCCTGTGTGGGCCATTGGTACTGGCAAGACTGCAACACCCCAA
CAGGCCCAGGAAGTACACGAGAAGCTCCGAGGATGGCTGAAGTCCAACGTCTCTGATGCG
GTGGCTCAGAGCACCCGTATCATTTATGGAGGCTCTGTGACTGGGGCAACCTGCAAGGAG
CTGGCCAGCCAGCCTGATGTGGATGGCTTCCTTGTGGGTGGTGCTTCCCTCAAGCCCGAA
TTCGTGGACATCATCAATGCCAAACAATGA
Enzyme 8 GenBank Gene ID M10036 Link Image
Enzyme 8 GeneCard ID TPI1 Link Image
Enzyme 8 GenAtlas ID TPI1 Link Image
Enzyme 8 HGNC ID HGNC:12009 Link Image
Enzyme 8 Chromosome Location 12
Enzyme 8 Locus 12p13
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Lu HS, Yuan PM, Gracy RW: Primary structure of human triosephosphate isomerase. J Biol Chem. 1984 Oct 10;259(19):11958-68. [PubMed Link Image]
  2. Maquat LE, Chilcote R, Ryan PM: Human triosephosphate isomerase cDNA and protein structure. Studies of triosephosphate isomerase deficiency in man. J Biol Chem. 1985 Mar 25;260(6):3748-53. [PubMed Link Image]
  3. Brown JR, Daar IO, Krug JR, Maquat LE: Characterization of the functional gene and several processed pseudogenes in the human triosephosphate isomerase gene family. Mol Cell Biol. 1985 Jul;5(7):1694-706. [PubMed Link Image]
  4. Ansari-Lari MA, Muzny DM, Lu J, Lu F, Lilley CE, Spanos S, Malley T, Gibbs RA: A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13. Genome Res. 1996 Apr;6(4):314-26. [PubMed Link Image]
  5. Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed Link Image]
  6. Rasmussen RK, Ji H, Eddes JS, Moritz RL, Reid GE, Simpson RJ, Dorow DS: Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. Electrophoresis. 1997 Mar-Apr;18(3-4):588-98. [PubMed Link Image]
  7. Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ: A two-dimensional gel database of human colon carcinoma proteins. Electrophoresis. 1997 Mar-Apr;18(3-4):605-13. [PubMed Link Image]
  8. Boyer TG, Krug JR, Maquat LE: Transcriptional regulatory sequences of the housekeeping gene for human triosephosphate isomerase. J Biol Chem. 1989 Mar 25;264(9):5177-87. [PubMed Link Image]
  9. Mande SC, Mainfroid V, Kalk KH, Goraj K, Martial JA, Hol WG: Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme. Protein Sci. 1994 May;3(5):810-21. [PubMed Link Image]
  10. Daar IO, Artymiuk PJ, Phillips DC, Maquat LE: Human triose-phosphate isomerase deficiency: a single amino acid substitution results in a thermolabile enzyme. Proc Natl Acad Sci U S A. 1986 Oct;83(20):7903-7. [PubMed Link Image]
  11. Perry BA, Mohrenweiser HW: Human triosephosphate isomerase: substitution of Arg for Gly at position 122 in a thermolabile electromorph variant, TPI-Manchester. Hum Genet. 1992 Mar;88(6):634-8. [PubMed Link Image]
  12. Chang ML, Artymiuk PJ, Wu X, Hollan S, Lammi A, Maquat LE: Human triosephosphate isomerase deficiency resulting from mutation of Phe-240. Am J Hum Genet. 1993 Jun;52(6):1260-9. [PubMed Link Image]
  13. Watanabe M, Zingg BC, Mohrenweiser HW: Molecular analysis of a series of alleles in humans with reduced activity at the triosephosphate isomerase locus. Am J Hum Genet. 1996 Feb;58(2):308-16. [PubMed Link Image]
  14. Arya R, Lalloz MR, Bellingham AJ, Layton DM: Evidence for founder effect of the Glu104Asp substitution and identification of new mutations in triosephosphate isomerase deficiency. Hum Mutat. 1997;10(4):290-4. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 13080
Enzyme 9 Name cDNA FLJ76204, highly similar to Homo sapiens transketolase
Enzyme 9 Synonyms
  1. Wernicke- Korsakoff syndrome
  2. TKT, mRNA
  3. Transketolase
  4. Wernicke-Korsakoff syndrome, isoform CRA_a
Enzyme 9 Gene Name TKT
Enzyme 9 Protein Sequence >cDNA FLJ76204, highly similar to Homo sapiens transketolase 
MESYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKS
QDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLNLRKISSDLDGHPVPKQAFTDV
ATGSLGQGLGAACGMAYTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNLVA
ILDINRLGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKHQPTAIIA
KTFKGRGITGVEDKESWHGKPLPKNMAEQIIQEIYSQIQSKKKILATPPQEDAPSVDIAN
IRMPSLPSYKVGDKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFI
ECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVS
IGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAII
YNNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPL
DRKLILDSARATKGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVNRVPRSGKPAE
LLKMFGIDRDAIAQAVRGLITKA
Enzyme 9 Number of Residues 623
Enzyme 9 Molecular Weight 67878
Enzyme 9 Theoretical pI 7.73
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Energy production and conversion
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function Not Available
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 158259931 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID A8K089 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name A8K089_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID AK289454 Link Image
Enzyme 9 GeneCard ID A8K089 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 15832
Enzyme 10 Name Triosephosphate isomerase (EC 5.3.1.1) (Fragment)
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name Not Available
Enzyme 10 Protein Sequence >Triosephosphate isomerase (EC 5.3.1.1) (Fragment) 
MAPSRKFFVGGNWKMNGRKQSLRELVRTLNAAKVPADTEVVCTPPTAYIDFARQKLDPKI
AVAAQNCYKVTNGAFTGEISPGMIKDCRATWVVLGHSERRHVFGESDELIGQKVAHALAE
GLGVIACTGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQ
QDQEVHDKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPGVDGFLVGGASLKPE
FVDIINAKQ
Enzyme 10 Number of Residues 249
Enzyme 10 Molecular Weight 26943
Enzyme 10 Theoretical pI 8.21
Enzyme 10 GO Classification
Function
  • catalytic activity
  • intramolecular oxidoreductase activity
  • intramolecular oxidoreductase activity, interconverting aldoses and ketoses
  • isomerase activity
  • triose-phosphate isomerase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 10 General Function Carbohydrate transport and metabolism
Enzyme 10 Specific Function D-glyceraldehyde 3-phosphate = glycerone phosphate
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions
  • D-glyceraldehyde 3-phosphate = glycerone phosphate [RN:R01015] ALL_REAC R01015
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
Enzyme 10 UniProtKB/Swiss-Prot ID Q2QD09 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name Q2QD09_HUMAN Link Image
Enzyme 10 PDB ID 1HTI Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID DQ120711 Link Image
Enzyme 10 GeneCard ID Q2QD09 Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs Not Available
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 16909
Enzyme 11 Name Glyceraldehyde 3-phosphate dehydrogenase
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name GAPD
Enzyme 11 Protein Sequence >Glyceraldehyde 3-phosphate dehydrogenase 
MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTV
KAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVI
ISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHA
ITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV
SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAG
IALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE
Enzyme 11 Number of Residues 335
Enzyme 11 Molecular Weight 36054
Enzyme 11 Theoretical pI 8.73
Enzyme 11 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity
  • glyceraldehyde-3-phosphate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 11 General Function Carbohydrate transport and metabolism
Enzyme 11 Specific Function D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID Q53X65 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name Q53X65_HUMAN Link Image
Enzyme 11 PDB ID 1J0X Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID CR407671 Link Image
Enzyme 11 GeneCard ID Q53X65 Link Image
Enzyme 11 GenAtlas ID GAPD Link Image
Enzyme 11 HGNC ID HGNC:4141 Link Image
Enzyme 11 Chromosome Location 12
Enzyme 11 Locus 12p13
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 16910
Enzyme 12 Name Glyceraldehyde 3-phosphate dehydrogenase
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name Not Available
Enzyme 12 Protein Sequence >Glyceraldehyde 3-phosphate dehydrogenase 
MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTV
KAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVI
ISTPSADAPMLVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHA
ITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV
SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAG
IALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE
Enzyme 12 Number of Residues 335
Enzyme 12 Molecular Weight 36050
Enzyme 12 Theoretical pI 8.73
Enzyme 12 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity
  • glyceraldehyde-3-phosphate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 12 General Function Carbohydrate transport and metabolism
Enzyme 12 Specific Function D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
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 Q2TSD0 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name Q2TSD0_HUMAN Link Image
Enzyme 12 PDB ID 1J0X Link Image
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 AY633612 Link Image
Enzyme 12 GeneCard ID Q2TSD0 Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID HGNC:4141 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs Not Available
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 16911
Enzyme 13 Name Triosephosphate isomerase
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name TPI1
Enzyme 13 Protein Sequence >Triosephosphate isomerase 
MAPSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKI
AVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAE
GLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQ
QAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE
FVDIINAKQ
Enzyme 13 Number of Residues 249
Enzyme 13 Molecular Weight 26670
Enzyme 13 Theoretical pI 6.91
Enzyme 13 GO Classification
Function
  • catalytic activity
  • intramolecular oxidoreductase activity
  • intramolecular oxidoreductase activity, interconverting aldoses and ketoses
  • isomerase activity
  • triose-phosphate isomerase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 13 General Function Carbohydrate transport and metabolism
Enzyme 13 Specific Function D-glyceraldehyde 3-phosphate = glycerone phosphate
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein Not Available
Enzyme 13 UniProtKB/Swiss-Prot ID Q6FHP9 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name Q6FHP9_HUMAN Link Image
Enzyme 13 PDB ID 1HTI Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence Not Available
Enzyme 13 GenBank Gene ID AK313282 Link Image
Enzyme 13 GeneCard ID Q6FHP9 Link Image
Enzyme 13 GenAtlas ID TPI1 Link Image
Enzyme 13 HGNC ID HGNC:12009 Link Image
Enzyme 13 Chromosome Location 12
Enzyme 13 Locus 12p13
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available