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Human Metabolome Database Version 2.5

 

Showing metabocard for Alpha-D-Glucose 1,6-bisphosphate (HMDB03514)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-12 23:34:16
Update Date 2009-08-18 12:49:03
Accession Number HMDB03514
Secondary Accession Numbers Not Available
Common Name Alpha-D-Glucose 1,6-bisphosphate
Description Glucose 1,6-diphosphate is considered to be a major regulator of carbohydrate metabolism. It has been demonstrated that G-1,6-P2 is a potent activator (deinhibitor) of skeletal muscle phosphofructokinase (PFK) and phosphoglucomutase, while being an inhibitor of hexokinase (see Ref. 2). In addition, G-1,6 P2 has been shown to inhibit 6-phosphogluconate dehydrogenase in various rat tissues and fructose 1,6-bisphosphatase in bovine liver. Various factors and conditions affect the tissue content of G-1,6-P2. Specifically, anoxia induce a rapid fall in the content of G-l,6-P2 in brain. Glucose 1,6-diphosphate (G 1,6-P2 )have been recognized as a regulatory signal implicated in the control of metabolism, oxygen affinity of red cells and other cellular functions. The levels of G 1,6-P2 are reduced in the liver and in the muscle of rats with experimentally induced diabetes. In muscle of genetically dystrophic mice a decrease in the levels of G 1,6-P2 has been found, probably resulting from enhancement of glucose 1,6-P2 phosphatase activity. G 1,6-P2 is an inhibitor of hexokinase and its level is increased significantly after 5 min of exercise (~ 25%) and then decreased continuously. G 1,6-P2 is a potent allosteric activator of phosphofructokinase, and is markedly decreased in muscles of patients with glycogenosis type VII (muscle phosphofructokinase deficiency) and type V (muscle phosphorylase deficiency). Chronic alcohol intake produces an increase in the concentration of G 1,6-P2 in human muscle before the first sign of myopathy appears. When myopathy is present the level decreases to be similar of healthy humans. These changes could contribute to the decline in skeletal muscle performance. (PMID: 1449560, 2018547, 2003594, 3407759)
Synonyms
  1. Alpha-D-1,6-bis(dihydrogen phosphate) Glucopyranose
  2. Glucose 1,6-diphosphate
  3. a-D-Glucose 1,6-bis(dihydrogen phosphate)
  4. a-D-Glucose 1,6-bisphosphate
  5. a-D-Glucose 1,6-diphosphate
  6. D-Glucose 1,6-diphosphate
  7. Glucose 1,6-bisphosphate
  8. Alpha-delta-1,6-bis(dihydrogen phosphate) Glucopyranose
  9. alpha-delta-Glucose 1,6-bis(dihydrogen phosphate)
  10. alpha-delta-Glucose 1,6-bisphosphate
  11. alpha-delta-Glucose 1,6-diphosphate
  12. delta-Glucose 1,6-diphosphate
  13. alpha-D-Glucose 1,6-bis(dihydrogen phosphate)
  14. alpha-D-Glucose 1,6-bisphosphate
  15. alpha-D-Glucose 1,6-diphosphate
Chemical IUPAC Name [(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(phosphonooxymethyl)oxan-2-yl]oxyphosphonic acid
Chemical Formula C6H14O12P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Sugar Phosphates
Sub Class
  • Monosaccharide phosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • phosphoric acid ester
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 340.116
Monoisotopic Molecular Weight 339.996063
Isomeric SMILES O[C@H]1[C@H](O)[C@@H](COP(O)(O)=O)O[C@H](OP(O)(O)=O)[C@@H]1O
Canonical SMILES OC1C(O)C(COP(O)(O)=O)OC(OP(O)(O)=O)C1O
KEGG Compound ID C01231 Link Image
BioCyc ID ALPHA-GLUCOSE-16-BISPHOSPHATE Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB03514 Link Image
Metagene Link HMDB03514 Link Image
METLIN ID Not Available
PubChem Compound 82400 Link Image
PubChem Substance 10219373 Link Image
ChEBI ID 18148 Link Image
CAS Registry Number 10139-18-1
InChI Identifier InChI=1/C6H14O12P2/c7-3-2(1-16-19(10,11)12)17-6(5(9)4(3)8)18-20(13,14)15/h2-9H,1H2,(H2,10,11,12)(H2,13,14,15)/t2-,3-,4+,5-,6-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 16.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity -4.374 Source: PhysProp
Predicted LogP/Hydrophobicity -1.65 [Predicted by ALOGPS]; -5.2 [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 Not Available
Biofluid Location
  • Blood
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 98.0 +/- 17.0 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.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Starch and Sucrose Metabolism SMP00058 Link Image map00500 Link Image
General References Not Available
Metabolic Enzymes
  1. Cytochrome c oxidase subunit 5A, mitochondrial precursor
  2. Phosphoglucomutase-2
  3. Glucose 1,6-bisphosphate synthase
  4. cDNA FLJ75943, highly similar to Homo sapiens phosphomannomutase 1 (PMM1), mRNA (Phosphomannomutase 1, isoform CRA_a)
  5. cDNA FLJ78512, highly similar to Homo sapiens phosphomannomutase 2 (PMM2), mRNA (Phosphomannomutase 2, isoform CRA_b)
Enzyme 1 [top]
Enzyme 1 ID 8647
Enzyme 1 Name Cytochrome c oxidase subunit 5A, mitochondrial precursor
Enzyme 1 Synonyms
  1. Cytochrome c oxidase polypeptide Va
Enzyme 1 Gene Name COX5A
Enzyme 1 Protein Sequence >Cytochrome c oxidase subunit 5A, mitochondrial precursor 
MLGAALRRCAVAATTRADPRGLLHSARTPGPAVAIQSVRCYSHGSQETDEEFDARWVTYF
NKPDIDAWELRKGINTLVTYDMVPEPKIIDAALRACRRLNDFASLVRILEVVKDKAGPHK
EIYPYVIQELRPTLNELGISTPEELGLDKV
Enzyme 1 Number of Residues 150
Enzyme 1 Molecular Weight 16774
Enzyme 1 Theoretical pI 6.78
Enzyme 1 GO Classification
Function
  • catalytic activity
  • cytochrome-c oxidase activity
  • heme-copper terminal oxidase activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 4 ferrocytochrome c + O2 = 4 ferricytochrome c + 2 H2O
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-17
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 695360 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P20674 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name COX5A_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >453 bp 
ATGCTGGGCGCCGCTCTCCGCCGCTGCGCTGTGGCCGCAACCACCCGGGCCGACCCTCGA
GGCCTCCTGCACTCCGCCCGGACCCCCGGCCCCGCCGTGGCTATCCAGTCAGTTCGCTGC
TATTCCCATGGGTCACAGGAGACAGATGAGGAGTTTGATGCTCGCTGGGTAACATACTTC
AACAAGCCAGATATAGATGCCTGGGAATTGCGTAAAGGGATAAACACACTTGTTACCTAT
GATATGGTTCCAGAGCCCAAAATCATTGATGCTGCTTTGCGGGCATGCAGACGGTTAAAT
GATTTTGCTAGTCTAGTTCGAATCCTAGAGGTTGTTAAGGACAAAGCAGGACCTCATAAG
GAAATCTACCCCTATGTCATCCAGGAACTTAGACCAACTTTAAATGAACTGGGAATCTCC
ACTCCGGAGGAACTGGGCCTTGACAAAGTGTAA
Enzyme 1 GenBank Gene ID M22760 Link Image
Enzyme 1 GeneCard ID COX5A Link Image
Enzyme 1 GenAtlas ID COX5A Link Image
Enzyme 1 HGNC ID HGNC:2267 Link Image
Enzyme 1 Chromosome Location 15
Enzyme 1 Locus 15q25
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Rizzuto R, Nakase H, Zeviani M, DiMauro S, Schon EA: Subunit Va of human and bovine cytochrome c oxidase is highly conserved. Gene. 1988 Sep 30;69(2):245-56. [PubMed Link Image]
  2. Hughes GJ, Frutiger S, Paquet N, Pasquali C, Sanchez JC, Tissot JD, Bairoch A, Appel RD, Hochstrasser DF: Human liver protein map: update 1993. Electrophoresis. 1993 Nov;14(11):1216-22. [PubMed Link Image]
  3. 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]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 9329
Enzyme 2 Name Phosphoglucomutase-2
Enzyme 2 Synonyms
  1. Glucose phosphomutase 2
  2. PGM 2
Enzyme 2 Gene Name PGM2
Enzyme 2 Protein Sequence >Phosphoglucomutase-2 
MAAPEGSGLGEDARLDQETAQWLRWDKNSLTLEAVKRLIAEGNKEELRKCFGARMEFGTA
GLRAAMGPGISRMNDLTIIQTTQGFCRYLEKQFSDLKQKGIVISFDARAHPSSGGSSRRF
ARLAATTFISQGIPVYLFSDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDN
GAQIISPHDKGISQAIEENLEPWPQAWDDSLIDSSPLLHNPSASINNDYFEDLKKYCFHR
SVNRETKVKFVHTSVHGVGHSFVQSAFKAFDLVPPEAVPEQKDPDPEFPTVKYPNPEEGK
GVLTLSFALADKTKARIVLANDPDADRLAVAEKQDSGEWRVFSGNELGALLGWWLFTSWK
EKNQDRSALKDTYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAKQLIDQGKTVL
FAFEEAIGYMCCPFVLDKDGVSAAVISAELASFLATKNLSLSQQLKAIYVEYGYHITKAS
YFICHDQETIKKLFENLRNYDGKNNYPKACGKFEISAIRDLTTGYDDSQPDKKAVLPTSK
SSQMITFTFANGGVATMRTSGTEPKIKYYAELCAPPGNSDPEQLKKELNELVSAIEEHFF
QPQKYNLQPKAD
Enzyme 2 Number of Residues 612
Enzyme 2 Molecular Weight 68284
Enzyme 2 Theoretical pI Not Available
Enzyme 2 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Carbohydrate transport and metabolism
Enzyme 2 Specific Function This enzyme participates in both the breakdown and synthesis of glucose
Enzyme 2 Pathways
Enzyme 2 Reactions
  • D-Glucose 1-phosphate <==> D-Glucose 6-phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 12052930 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q96G03 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PGM2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence Not Available
Enzyme 2 GenBank Gene ID AL136705 Link Image
Enzyme 2 GeneCard ID Not Available
Enzyme 2 GenAtlas ID PGM2 Link Image
Enzyme 2 HGNC ID HGNC:8906 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. 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 Link Image]
  2. 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]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 14947
Enzyme 3 Name Glucose 1,6-bisphosphate synthase
Enzyme 3 Synonyms
  1. Phosphoglucomutase-2-like 1
  2. PMMLP
Enzyme 3 Gene Name PGM2L1
Enzyme 3 Protein Sequence >Glucose 1,6-bisphosphate synthase 
MAENTEGDLNSNLLHAPYHTGDPQLDTAIGQWLRWDKNPKTKEQIENLLRNGMNKELRDR
LCCRMTFGTAGLRSAMGAGFCYINDLTVIQSTQGMYKYLERCFSDFKQRGFVVGYDTRGQ
VTSSCSSQRLAKLTAAVLLAKDVPVYLFSRYVPTPFVPYAVQKLKAVAGVMITASHNRKE
DNGYKVYWETGAQITSPHDKEILKCIEECVEPWNGSWNDNLVDTSPLKRDPLQDICRRYM
EDLKKICFYRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFKPPIPVPEQKDPDPDFST
VKCPNPEEGESVLELSLRLAEKENARVVLATDPDADRLAAAELQENGCWKVFTGNELAAL
FGWWMFDCWKKNKSRNADVKNVYMLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRII
DLLENGKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASYLETMNITLKQQLVKVYE
KYGYHISKTSYFLCYEPPTIKSIFERLRNFDSPKEYPKFCGTFAILHVRDITTGYDSSQP
NKKSVLPVSKNSQMITFTFQNGCVATLRTSGTEPKIKYYAEMCASPDQSDTALLEEELKK
LIDALIENFLQPSKNGLIWRSV
Enzyme 3 Number of Residues 622
Enzyme 3 Molecular Weight 70456
Enzyme 3 Theoretical pI 7.17
Enzyme 3 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Carbohydrate transport and metabolism
Enzyme 3 Specific Function Glucose 1,6-bisphosphate synthase using 1,3- bisphosphoglycerate as a phosphate donor and a series of 1- phosphate sugars as acceptors, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1- phosphate. 5 or 6-phosphosugars are bad substrates, with the exception of glucose 6-phosphate. Also synthesizes ribose 1,5- bisphosphate. Has only low phosphopentomutase and phosphoglucomutase activities
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 5688958 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q6PCE3 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PGM2L_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1869 bp 
ATGGCTGAAAACACAGAGGGGGATCTGAACTCCAACCTGCTCCACGCCCCCTACCACACC
GGGGACCCTCAGCTGGACACGGCCATCGGGCAGTGGCTCCGCTGGGATAAGAATCCCAAA
ACAAAAGAGCAGATTGAAAACCTGTTACGGAATGGGATGAACAAGGAGCTGCGAGATCGT
CTTTGTTGCCGAATGACTTTTGGGACTGCAGGACTTCGTTCTGCCATGGGGGCAGGGTTT
TGCTATATTAATGACCTTACAGTAATACAGTCAACACAGGGGATGTACAAATACCTTGAG
AGATGTTTCTCAGACTTCAAGCAGAGAGGCTTTGTGGTTGGGTATGACACTCGGGGTCAA
GTAACTAGCAGCTGCAGCAGCCAGAGGCTTGCTAAACTCACTGCTGCAGTCTTGCTGGCC
AAAGATGTTCCTGTGTACCTTTTTTCAAGATATGTTCCTACACCTTTTGTACCATATGCA
GTTCAGAAGCTCAAAGCAGTTGCAGGTGTGATGATTACTGCCTCTCACAACCGCAAGGAA
GACAATGGATACAAGGTTTACTGGGAAACTGGTGCTCAGATCACATCTCCTCATGATAAA
GAAATTCTAAAATGTATAGAAGAATGTGTGGAACCCTGGAATGGTTCCTGGAATGATAAT
TTAGTGGATACCAGCCCGCTGAAGAGAGACCCTCTGCAGGACATTTGCAGGAGATACATG
GAAGATCTGAAAAAGATCTGTTTTTACAGGGAGTTAAACTCGAAGACCACCTTGAAATTT
GTGCACACATCTTTTCATGGGGTCGGACATGACTATGTGCAGTTGGCTTTTAAAGTGTTT
GGTTTTAAGCCTCCAATTCCAGTACCAGAACAAAAAGATCCTGATCCAGACTTTTCTACC
GTTAAATGTCCAAATCCTGAAGAAGGAGAATCTGTGCTGGAACTTTCCTTGAGACTGGCA
GAGAAAGAAAATGCCCGGGTAGTGCTAGCCACAGATCCTGATGCAGACAGACTGGCAGCA
GCAGAACTTCAGGAGAATGGTTGTTGGAAAGTTTTCACAGGGAATGAGTTGGCAGCTTTG
TTTGGATGGTGGATGTTTGATTGCTGGAAGAAAAATAAATCAAGAAATGCTGATGTGAAG
AACGTTTATATGTTAGCCACCACAGTCTCTTCTAAAATTCTGAAGGCAATTGCACTTAAA
GAAGGATTTCATTTTGAAGAAACATTACCAGGTTTTAAATGGATTGGAAGTAGGATAATA
GACCTCCTGGAAAATGGGAAAGAAGTCCTTTTTGCATTTGAAGAGTCTATTGGTTTTCTC
TGTGGAACTTCAGTTTTGGATAAAGATGGGGTGAGTGCAGCTGTTGTGGTTGCTGAGATG
GCATCTTACCTGGAAACCATGAATATAACATTGAAACAGCAACTGGTTAAGGTTTATGAA
AAATATGGTTATCATATTTCAAAAACTTCCTATTTCTTGTGTTATGAACCACCTACCATC
AAAAGTATATTTGAAAGGCTTCGTAATTTTGATTCTCCAAAAGAATATCCAAAATTTTGT
GGAACATTTGCTATATTGCATGTACGGGACGTTACCACTGGATATGACAGTAGCCAGCCT
AATAAGAAATCAGTGCTGCCTGTGAGTAAAAACAGCCAAATGATTACATTTACTTTTCAA
AATGGCTGTGTTGCTACCCTTCGGACAAGTGGAACAGAACCAAAGATAAAGTATTATGCA
GAGATGTGTGCGTCACCTGACCAGAGTGACACTGCTTTACTGGAGGAAGAACTGAAGAAA
CTCATTGATGCTCTGATAGAGAATTTTCTTCAGCCTAGTAAGAATGGACTGATCTGGCGT
TCTGTTTAG
Enzyme 3 GenBank Gene ID AB019210 Link Image
Enzyme 3 GeneCard ID Q6PCE3 Link Image
Enzyme 3 GenAtlas ID PGM2L1 Link Image
Enzyme 3 HGNC ID HGNC:20898 Link Image
Enzyme 3 Chromosome Location 11
Enzyme 3 Locus 11q13.4
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 15878
Enzyme 4 Name cDNA FLJ75943, highly similar to Homo sapiens phosphomannomutase 1 (PMM1), mRNA (Phosphomannomutase 1, isoform CRA_a)
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name PMM1
Enzyme 4 Protein Sequence >cDNA FLJ75943, highly similar to Homo sapiens phosphomannomutase 1 (PMM1), mRNA (Phosphomannomutase 1, isoform CRA_a) 
MAVTAQAARRKERVLCLFDVDGTLTPARQKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIA
EQLGDGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFCLSYMALLR
LPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLR
FSRGGMISFDVFPEGWDKRYCLDSLDQDSFDTIHFFGNETSPGGNDFEIFADPRTVGHSV
VSPQDTVQRCREIFFPETAHEA
Enzyme 4 Number of Residues 262
Enzyme 4 Molecular Weight 29747
Enzyme 4 Theoretical pI 5.47
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function Not Available
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID A8K003 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A8K003_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AK289368 Link Image
Enzyme 4 GeneCard ID A8K003 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location 22
Enzyme 4 Locus 22q13.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 15879
Enzyme 5 Name cDNA FLJ78512, highly similar to Homo sapiens phosphomannomutase 2 (PMM2), mRNA (Phosphomannomutase 2, isoform CRA_b)
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name PMM2
Enzyme 5 Protein Sequence >cDNA FLJ78512, highly similar to Homo sapiens phosphomannomutase 2 (PMM2), mRNA (Phosphomannomutase 2, isoform CRA_b) 
MAAPGPALCLFDVDGTLTAPRQKITKEMDDFLQKLRQKIKIGVVGGSDFEKVQEQLGNDV
VEKYDYVFPENGLVAYKDGKLLCRQNIQSHLGEALIQDLINYCLSYIAKIKLPKKRGTFI
EFRNGMLNVSPIGRSCSQEERIEFYELDKKENIRQKFVADLRKEFAGKGLTFSIGGQISF
DVFPDGWDKRYCLRHVENDGYKTIYFFGDKTMPGGNDHEIFTDPRTMGYSVTAPEDTRRI
CELLFS
Enzyme 5 Number of Residues 246
Enzyme 5 Molecular Weight 28082
Enzyme 5 Theoretical pI 6.76
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function Not Available
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID A8K672 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name A8K672_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK291537 Link Image
Enzyme 5 GeneCard ID A8K672 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location 16
Enzyme 5 Locus 16p13.3-p13.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available