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Human Metabolome Database Version 2.5

 

Showing metabocard for 2-Phospho-D-glyceric acid (HMDB03391)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-12 21:03:00
Update Date 2009-05-05 20:59:36
Accession Number HMDB03391
Secondary Accession Numbers Not Available
Common Name 2-Phospho-D-glyceric acid
Description 2-Phospho-D-glycerate or 2PG is an intermediate in gluconeogenesis. It is a glyceric acid which serves as the substrate in the ninth step of glycolysis. 2PG is converted by enolase into phosphoenolpyruvate (PEP), the penultimate step in the conversion of glucose to pyruvate. More specifically, 2PG can be generated from Glycerate-3-phosphate via phosphoglycerate mutase or from phosphoenolpyrvate via alpha enolase.
Synonyms
  1. 2-Phospho-D-glycerate
  2. 2-Phospho-D-glyceric acid
  3. D-Glycerate 2-phosphate
  4. 3-D-Hydroxy-2-phosphonooxy-propanoic acid
  5. (2R)-3-hydroxy-2-(phosphonooxy)propanoic acid
  6. 3-D-Hydroxy-2-phosphonooxy-propanoate
  7. (2R)-3-hydroxy-2-(phosphonooxy)propanoate
Chemical IUPAC Name (2R)-3-hydroxy-2-phosphonooxy-propanoic acid
Chemical Formula C3H7O7P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Miscellaneous
Class
  • Acyl Phosphates
Sub Class
  • Glycerophosphates
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • carboxylic acid
  • phosphoric acid ester
Biofunction
  • Component of Phenylalanine, tyrosine and tryptophan biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 186.057
Monoisotopic Molecular Weight 185.992935
Isomeric SMILES OC[C@@H](OP(O)(O)=O)C(O)=O
Canonical SMILES OCC(OP(O)(O)=O)C(O)=O
KEGG Compound ID C00631 Link Image
BioCyc ID 2-PG Link Image
BiGG ID 35542 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB03391 Link Image
Metagene Link HMDB03391 Link Image
METLIN ID 6915 Link Image
PubChem Compound 439278 Link Image
PubChem Substance 10317528 Link Image
ChEBI ID 17835 Link Image
CAS Registry Number Not Available
InChI Identifier InChI=1/C3H7O7P/c4-1-2(3(5)6)10-11(7,8)9/h2,4H,1H2,(H,5,6)(H2,7,8,9)/t2-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 20.3 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.24 [Predicted by ALOGPS]; -3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Gluconeogenesis SMP00128 Link Image map00010 Link Image
Glycolysis SMP00040 Link Image map00010 Link Image
General References Not Available
Metabolic Enzymes
  1. Phosphoglycerate mutase 2
  2. Phosphoglycerate mutase 1
  3. Beta-enolase
  4. Gamma-enolase
  5. Alpha-enolase
  6. Phosphoglycerate mutase family member 4 (PGAM3)
Enzyme 1 [top]
Enzyme 1 ID 5499
Enzyme 1 Name Phosphoglycerate mutase 2
Enzyme 1 Synonyms
  1. Phosphoglycerate mutase isozyme M
  2. PGAM-M
  3. BPG-dependent PGAM 2
  4. Muscle-specific phosphoglycerate mutase
Enzyme 1 Gene Name PGAM2
Enzyme 1 Protein Sequence >Phosphoglycerate mutase 2 
MATHRLVMVRHGESTWNQENRFCGWFDAELSEKGTEEAKRGAKAIKDAKMEFDICYTSVL
KRAIRTLWAILDGTDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEEQVKIWRRSFD
IPPPPMDEKHPYYNSISKERRYAGLKPGELPTCESLKDTIARALPFWNEEIVPQIKAGKR
VLIAAHGNSLRGIVKHLEGMSDQAIMELNLPTGIPIVYELNKELKPTKPMQFLGDEETVR
KAMEAVAAQGKAK
Enzyme 1 Number of Residues 253
Enzyme 1 Molecular Weight 28767
Enzyme 1 Theoretical pI 9.32
Enzyme 1 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
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 Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 189872 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P15259 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PGAM2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >762 bp 
ATGGCCACTCACCGCCTCGTGATGGTCCGGCACGGCGAGAGCACATGGAACCAGGAGAAC
CGTTTCTGTGGCTGGTTCGATGCAGAGCTGAGTGAAAAGGGGACCGAGGAGGCCAAGCGG
GGAGCCAAGGCCATCAAGGATGCCAAGATGGAGTTTGACATCTGCTACACGTCAGTGCTG
AAGCGGGCCATCCGCACCCTCTGGGCCATCCTGGACGGCACGGACCAGATGTGGCTGCCT
GTGGTGCGCACTTGGCGCCTCAATGAGCGGCATTACGGGGGCCTCACAGGCCTCAACAAG
GCAGAAACGGCCGCCAAGCACGGGGAGGAGCAGGTGAAGATCTGGAGGCGCTCCTTCGAC
ATCCCGCCGCCCCCGATGGACGAGAAGCACCCCTACTACAACTCCATTAGCAAGGAGCGT
CGGTACGCAGGCCTGAAGCCCGGGGAACTCCCCACCTGCGAGAGCCTCAAGGACACCATT
GCCCGGGCCCTGCCCTTCTGGAACGAGGAGATTGTTCCCCAGATCAAGGCCGGCAAGCGA
GTGCTCATTGCAGCCCACGGGAACAGCCTGCGGGGCATTGTCAAGCACCTGGAAGGGATG
TCAGACCAGGCGATCATGGAGCTGAACCTGCCCACGGGGATCCCCATTGTGTATGAGCTG
AACAAGGAGCTGAAGCCCACCAAGCCCATGCAGTTCCTGGGTGATGAGGAAACGGTGCGG
AAGGCCATGGAGGCTGTGGCTGCCCAGGGCAAGGCCAAGTGA
Enzyme 1 GenBank Gene ID M55674 Link Image
Enzyme 1 GeneCard ID PGAM2 Link Image
Enzyme 1 GenAtlas ID PGAM2 Link Image
Enzyme 1 HGNC ID HGNC:8889 Link Image
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Castella-Escola J, Ojcius DM, LeBoulch P, Joulin V, Blouquit Y, Garel MC, Valentin C, Rosa R, Climent-Romeo F, Cohen-Solal M: Isolation and characterization of the gene encoding the muscle-specific isozyme of human phosphoglycerate mutase. Gene. 1990 Jul 16;91(2):225-32. [PubMed Link Image]
  2. Tsujino S, Sakoda S, Mizuno R, Kobayashi T, Suzuki T, Kishimoto S, Shanske S, DiMauro S, Schon EA: Structure of the gene encoding the muscle-specific subunit of human phosphoglycerate mutase. J Biol Chem. 1989 Sep 15;264(26):15334-7. [PubMed Link Image]
  3. Shanske S, Sakoda S, Hermodson MA, DiMauro S, Schon EA: Isolation of a cDNA encoding the muscle-specific subunit of human phosphoglycerate mutase. J Biol Chem. 1987 Oct 25;262(30):14612-7. [PubMed Link Image]
  4. Tsujino S, Shanske S, Sakoda S, Fenichel G, DiMauro S: The molecular genetic basis of muscle phosphoglycerate mutase (PGAM) deficiency. Am J Hum Genet. 1993 Mar;52(3):472-7. [PubMed Link Image]
  5. Hadjigeorgiou GM, Kawashima N, Bruno C, Andreu AL, Sue CM, Rigden DJ, Kawashima A, Shanske S, DiMauro S: Manifesting heterozygotes in a Japanese family with a novel mutation in the muscle-specific phosphoglycerate mutase (PGAM-M) gene. Neuromuscul Disord. 1999 Oct;9(6-7):399-402. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5501
Enzyme 2 Name Phosphoglycerate mutase 1
Enzyme 2 Synonyms
  1. Phosphoglycerate mutase isozyme B
  2. PGAM-B
  3. BPG-dependent PGAM 1
Enzyme 2 Gene Name PGAM1
Enzyme 2 Protein Sequence >Phosphoglycerate mutase 1 
MAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQ
KRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYD
VPPPPMEPDHPFYSNISKDRRYADLTEDQLPSCESLKDTIARALPFWNEEIVPQIKEGKR
VLIAAHGNSLRGIVKHLEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVR
KAMEAVAAQGKAKK
Enzyme 2 Number of Residues 254
Enzyme 2 Molecular Weight 28804
Enzyme 2 Theoretical pI 7.22
Enzyme 2 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
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 Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 551174 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P18669 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PGAM1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >765 bp 
ATGGCCGCCTACAAACTGGTGCTGATCCGGCACGGCGAGAGCGCATGGAACCTGGAGAAC
CGCTTCAGCGGCTGGTACGACGCCGACCTGAGCCCGGCGGGCCACGAGGAGGCGAAGCGC
GGCGGGCAGGCGCTACGAGATGCTGGCTATGAGTTTGACATCTGCTTCACCTCAGTGCAG
AAGAGAGCGATCCGGACCCTCTGGACAGTGCTAGATGCCATTGATCAGATGTGGCTGCCA
GTGGTGAGGACTTGGCGCCTCAATGAGCGGCACTATGGGGGTCTAACCGGTCTCAATAAA
GCAGAAACTGCTGCAAAGCATGGTGAGGCCCAGGTGAAGATCTGGAGGCGCTCCTATGAT
GTCCCACCACCTCCGATGGAGCCCGACCATCCTTTCTACAGCAACATCAGTAAGGATCGC
AGGTATGCAGACCTCACAGAAGATCAGCTACCCTCCTGTGAGAGTCTGAAGGATACTATT
GCCAGAGCTCTGCCCTTCTGGAATGAAGAAATAGTTCCCCAGATCAAGGAGGGGAAACGT
GTACTGATTGCAGCCCATGGCAACAGCCTCCGGGGCATTGTCAAGCATCTGGAGGGTCTC
TCTGAAGAGGCTATCATGGAGCTGAACCTGCCGACTGGTATTCCCATTGTCTATGAATTG
GACAAGAACTTGAAGCCTATCAAGCCCATGCAGTTTCTGGGGGATGAAGAGACGGTGCGC
AAAGCCATGGAAGCTGTGGCTGCCCAGGGCAAGGCCAAGAAGTGA
Enzyme 2 GenBank Gene ID J04173 Link Image
Enzyme 2 GeneCard ID PGAM1 Link Image
Enzyme 2 GenAtlas ID PGAM1 Link Image
Enzyme 2 HGNC ID HGNC:8888 Link Image
Enzyme 2 Chromosome Location 10
Enzyme 2 Locus 10q25.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Sakoda S, Shanske S, DiMauro S, Schon EA: Isolation of a cDNA encoding the B isozyme of human phosphoglycerate mutase (PGAM) and characterization of the PGAM gene family. J Biol Chem. 1988 Nov 15;263(32):16899-905. [PubMed Link Image]
  2. Blouquit Y, Calvin MC, Rosa R, Prome D, Prome JC, Pratbernou F, Cohen-Solal M, Rosa J: Sequence of the human erythrocyte phosphoglycerate mutase by microsequencer and mass spectrometry. J Biol Chem. 1988 Nov 15;263(32):16906-10. [PubMed Link Image]
  3. 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]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6374
Enzyme 3 Name Beta-enolase
Enzyme 3 Synonyms
  1. 2-phospho-D-glycerate hydro-lyase
  2. Muscle-specific enolase
  3. MSE
  4. Skeletal muscle enolase
  5. Enolase 3
Enzyme 3 Gene Name ENO3
Enzyme 3 Protein Sequence >Beta-enolase 
MAMQKIFAREILDSRGNPTVEVDLHTAKGRFRAAVPSGASTGIYEALELRDGDKGRYLGK
GVLKAVENINNTLGPALLQKKLSVVDQEKVDKFMIELDGTENKSKFGANAILGVSLAVCK
AGAAEKGVPLYRHIADLAGNPDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFKE
AMRIGAEVYHHLKGVIKAKYGKDATNVGDEGGFAPNILENNEALELLKTAIQAAGYPDKV
VIGMDVAASEFYRNGKYDLDFKSPDDPARHITGEKLGELYKSFIKNYPVVSIEDPFDQDD
WATWTSFLSGVNIQIVGDDLTVTNPKRIAQAVEKKACNCLLLKVNQIGSVTESIQACKLA
QSNGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEALGDK
AIFAGRKFRNPKAK
Enzyme 3 Number of Residues 434
Enzyme 3 Molecular Weight 46987
Enzyme 3 Theoretical pI 7.84
Enzyme 3 GO Classification
Function
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • lyase activity
  • phosphopyruvate hydratase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
  • phosphopyruvate hydratase complex
  • protein complex
Enzyme 3 General Function Carbohydrate transport and metabolism
Enzyme 3 Specific Function Appears to have a function in striated muscle development and regeneration
Enzyme 3 Pathways
Enzyme 3 Reactions
  • 2-phospho-D-glycerate = phosphoenolpyruvate + H2O
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 31170 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P13929 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ENOB_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1305 bp 
ATGGCCATGCAGAAAATCTTTGCCCGGGAAATCTTGGACTCCAGGGGCAACCCCACGGTG
GAGGTGGACCTGCACACGGCCAAGGGCCGATTCCGAGCAGCTGTGCCCAGTGGGGCTTCC
ACGGGTATCTATGAGGCTCTGGAACTAAGAGACGGAGACAAAGGCCGCTACCTGGGGAAA
GGAGTCCTGAAGGCTGTGGAGAACATCAACAATACTCTGGGCCCTGCTCTGCTGCAAAAG
AAACTAAGCGTTGTTGATCAAGAAAAAGTTGACAAATTTATGATTGAGCTAGATGGGACC
GAGAATAAGTCCAAGTTTGGGGCCAATGCCATCCTGGGCGTGTCCTTGGCCGTGTGTAAG
GCGGGAGCAGCTGAGAAGGGGGTCCCCCTGTACCGCCACATCGCAGATCTCGCTGGGAAC
CCTGACCTCATACTCCCAGTGCCAGCCTTCAATGTGATCAACGGGGGCTCCCATGCTGGA
AACAACTTGGCCATGCAGGAGTTCATGATTCTGCCTGTGGGAGCCAGCTCCTTCAAGGAA
GCCATGCGCATTGGCGCCGAGGTCTACCACCACCTCAAGGGGGTCATCAAGGCCAAGTAT
GGGAAGGATGCCACCAATGTGGGTGATGAAGGTGGCTTCGCACCCAACATCCTGGAGAAC
AATGAGGCCCTGGAGCTGCTGAAGACGGCCATCCAGGCGGCTGGTTACCCAGACAAGGTG
GTGATCGGCATGGATGTGGCAGCATCTGAGTTCTATCGCAATGGGAAGTACGATCTTGAC
TTCAAGTCGCCTGATGATCCCGCACGGCACATCACTGGGGAGAAGCTCGGAGAGCTGTAT
AAGAGCTTTATCAAGAACTATCCTGTGGTCTCCATCGAAGACCCCTTTGACCAGGATGAC
TGGGCCACTTGGACCTCCTTCCTCTCGGGGGTGAACATCCAGATTGTGGGGGATGACTTG
ACAGTCACCAACCCCAAGAGGATTGCCCAGGCCGTTGAGAAGAAGGCCTGCAACTGTCTG
CTGCTGAAGGTCAACCAGATCGGCTCGGTGACCGAATCGATCCAGGCGTGCAAACTGGCT
CAGTCTAATGGCTGGGGGGTGATGGTGAGCCACCGCTCAGGGGAGACTGAGGACACATTC
ATTGCTGACCTTGTGGTGGGGCTCTGCACAGGACAGATCAAGACTGGCGCCCCCTGCCGC
TCGGAGCGTCTGGCCAAATACAACCAACTCATGAGGATCGAGGAGGCTCTTGGGGACAAG
GCAATCTTTGCTGGACGCAAGTTCCGTAACCCGAAGGCCAAGTGA
Enzyme 3 GenBank Gene ID X16504 Link Image
Enzyme 3 GeneCard ID ENO3 Link Image
Enzyme 3 GenAtlas ID ENO3 Link Image
Enzyme 3 HGNC ID HGNC:3354 Link Image
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17pter-p11
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Peshavaria M, Hinks LJ, Day IN: Structure of human muscle (beta) enolase mRNA and protein deduced from a genomic clone. Nucleic Acids Res. 1989 Nov 11;17(21):8862. [PubMed Link Image]
  2. Peshavaria M, Day IN: Molecular structure of the human muscle-specific enolase gene (ENO3). Biochem J. 1991 Apr 15;275 ( Pt 2):427-33. [PubMed Link Image]
  3. Cali L, Feo S, Oliva D, Giallongo A: Nucleotide sequence of a cDNA encoding the human muscle-specific enolase (MSE). Nucleic Acids Res. 1990 Apr 11;18(7):1893. [PubMed Link Image]
  4. Giallongo A, Venturella S, Oliva D, Barbieri G, Rubino P, Feo S: Structural features of the human gene for muscle-specific enolase. Differential splicing in the 5'-untranslated sequence generates two forms of mRNA. Eur J Biochem. 1993 Jun 1;214(2):367-74. [PubMed Link Image]
  5. Comi GP, Fortunato F, Lucchiari S, Bordoni A, Prelle A, Jann S, Keller A, Ciscato P, Galbiati S, Chiveri L, Torrente Y, Scarlato G, Bresolin N: Beta-enolase deficiency, a new metabolic myopathy of distal glycolysis. Ann Neurol. 2001 Aug;50(2):202-7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6375
Enzyme 4 Name Gamma-enolase
Enzyme 4 Synonyms
  1. 2-phospho-D-glycerate hydro-lyase
  2. Neural enolase
  3. Neuron-specific enolase
  4. NSE
  5. Enolase 2
Enzyme 4 Gene Name ENO2
Enzyme 4 Protein Sequence >Gamma-enolase 
MSIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDGDKQRYLGK
GVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCK
AGAAERELPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRD
AMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKI
VIGMDVAASEFYRDGKYDLDFKSPTDPSRYITGDQLGALYQDFVRDYPVVSIEDPFDQDD
WAAWSKFTANVGIQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLA
QENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEELGDE
ARFAGHNFRNPSVL
Enzyme 4 Number of Residues 434
Enzyme 4 Molecular Weight 47269
Enzyme 4 Theoretical pI 4.65
Enzyme 4 GO Classification
Function
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • lyase activity
  • phosphopyruvate hydratase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
  • phosphopyruvate hydratase complex
  • protein complex
Enzyme 4 General Function Carbohydrate transport and metabolism
Enzyme 4 Specific Function Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival
Enzyme 4 Pathways
Enzyme 4 Reactions
  • 2-phospho-D-glycerate = phosphoenolpyruvate + H2O
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 930063 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P09104 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name ENOG_HUMAN Link Image
Enzyme 4 PDB ID 1TE6 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1299 bp 
TCCATACAGAAGATCTGGGCCCGGGAGATCCTGGACTCCCGTGGGAACCCCACAGTGGAG
GTGGATCTCTATACTGCCAAAGGTCTTTTCCGGGCTGCAGTGCCCAGTGGAGCCTCTACG
GGCATCTATGAGGCCCTGGAGCTGAGGGATGGAGACAAACAGCGTTACTTAGGCAAAGGT
GTCCTGAAGGCAGTGGACCACATCAACTCCACCATCGCGCCAGCCCTCATCAGCTCAGGT
CTCTCTGTGGTGGAGCAAGAGAAGCTGGACAACCTGATGCTGGAGTTGGATGGGACTGAG
AACAAATCCAAGTTTGGGGCCAATGCCATCCTGGGTGTGTCTCTGGCCGTGTGTAAGGCA
GGGGCAGCTGAGCGGGAACTGCCCCTGTATCGCCACATTGCTCAGCTGGCCGGGAACTCA
GACCTCATCCTGCCTGTGCCGGCCTTCAACGTGATCAATGGTGGCTCTCATGCTGGCAAC
AAGCTGGCCATGCAGGAGTTCATGATCCTCCCAGTGGGAGCTGAGAGCTTTCGGGATGCC
ATGCGACTAGGTGCAGAGGTCTACCATACTCTCAAGGGAGTCATCAAGGACAAATACGGC
AAGGATGCCACCAATGTGGGGGATGAAGGTGGCTTTGCCCCCAATATCCTGGAGAACAGT
GAAGCCTTGGAGCTGGTTAAGGAAGCCATCGACAAGGCTGGCTACACGGAAAAAATGGTT
ATTGGCATGGATGTTGCTGCCTCAGAGTTTTATCGTGATGGCAAATATGACTTGGACTTC
AAGTCTCCCACTGATCCTTCCCGATACATCACTGGGGACCAGCTGGGGGCACTCTACCAG
GACTTTGTCAGGGACTATCCTGTGGTCTCCATTGAGGACCCATTTGACCAGGATGATTGG
GCTGCCTGGTCCAAGTTCACAGCCAATGTAGGGATCCAGATTGTGGGTGATGACCTGACA
GTGACCAACCCAAAACGTATTGAGCGGGCAGTGGAAGAAAAGGCCTGCAACTGTCTGCTG
CTCAAGGTCAACCAGATCGGCTCGGTCACTGAAGCCATCCAAGCGTGCAAGCTGGCCCAG
GAGAATGGCTGGGGGGTCATGGTGAGTCATCGCTCAGGAGAGACTGAGGACACATTCATT
GCTGACCTGGTGGTGGGGCTGTGCACAGGCCAGATCAAGACTGGTGCCCCGTGCCGTTCT
GAACGTCTGGCTAAATACAATCAGCTCATGAGAATTGAGGAAGAGCTGGGGGATGAAGCT
CGCTTTGCCGGACATAACTTCCGTAATCCCAGTGTGCTG
Enzyme 4 GenBank Gene ID X13120 Link Image
Enzyme 4 GeneCard ID ENO2 Link Image
Enzyme 4 GenAtlas ID ENO2 Link Image
Enzyme 4 HGNC ID HGNC:3353 Link Image
Enzyme 4 Chromosome Location 12
Enzyme 4 Locus 12p13
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. McAleese SM, Dunbar B, Fothergill JE, Hinks LJ, Day IN: Complete amino acid sequence of the neurone-specific gamma isozyme of enolase (NSE) from human brain and comparison with the non-neuronal alpha form (NNE). Eur J Biochem. 1988 Dec 15;178(2):413-7. [PubMed Link Image]
  2. Oliva D, Barba G, Barbieri G, Giallongo A, Feo S: Cloning, expression and sequence homologies of cDNA for human gamma enolase. Gene. 1989 Jul 15;79(2):355-60. [PubMed Link Image]
  3. Van Obberghen E, Kamholz J, Bishop JG 3rd, Zomzely-Neurath C, Lazzarini RA, Lazzarini RA: Human gamma enolase: isolation of a cDNA clone and expression in normal and tumor tissues of human origin. J Neurosci Res. 1988 Apr;19(4):450-6. [PubMed Link Image]
  4. Oliva D, Cali L, Feo S, Giallongo A: Complete structure of the human gene encoding neuron-specific enolase. Genomics. 1991 May;10(1):157-65. [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. Day IN, Allsopp MT, Moore DC, Thompson RJ: Sequence conservation in the 3'-untranslated regions of neurone-specific enolase, lymphokine and protooncogene mRNAs. FEBS Lett. 1987 Sep 28;222(1):139-43. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6376
Enzyme 5 Name Alpha-enolase
Enzyme 5 Synonyms
  1. 2-phospho-D-glycerate hydro-lyase
  2. Non- neural enolase
  3. NNE
  4. Enolase 1
  5. Phosphopyruvate hydratase
  6. C-myc promoter-binding protein
  7. MBP-1
  8. MPB-1
  9. Plasminogen-binding protein
Enzyme 5 Gene Name ENO1
Enzyme 5 Protein Sequence >Alpha-enolase 
MSILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGASTGIYEALELRDNDKTRYMGK
GVSKAVEHINKTIAPALVSKKLNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCK
AGAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGAANFRE
AMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKV
VIGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDD
WGAWQKFTASAGIQVVGDDLTVTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLA
QANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRIEEELGSK
AKFAGRNFRNPLAK
Enzyme 5 Number of Residues 434
Enzyme 5 Molecular Weight 47169
Enzyme 5 Theoretical pI 7.46
Enzyme 5 GO Classification
Function
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • lyase activity
  • phosphopyruvate hydratase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
  • phosphopyruvate hydratase complex
  • protein complex
Enzyme 5 General Function Carbohydrate transport and metabolism
Enzyme 5 Specific Function MBP1 binds to the c-myc promoter and acts as a transcriptional repressor. May be a tumor suppressor
Enzyme 5 Pathways
Enzyme 5 Reactions
  • 2-phospho-D-glycerate = phosphoenolpyruvate + H2O
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 182114 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P06733 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name ENOA_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1305 bp 
ATGTCTATTCTCAAGATCCATGCCAGGGAGATCTTTGACTCTCGCGGGAATCCCACTGTT
GAGGTTGATCTCTTCACCTCAAAAGGTCTCTTCAGAGCTGCTGTGCCCAGTGGTGCTTCA
ACTGGTATCTATGAGGCCCTAGAGCTCCGGGACAATGATAAGACTCGCTATATGGGGAAG
GGTGTCTCAAAGGCTGTTGAGCACATCAATAAAACTATTGCGCCTGCCCTGGTTAGCAAG
AAACTGAACGTCACAGAACAAGAGAAGATTGACAAACTGATGATCGAGATGGATGGAACA
GAAAATAAATCTAAGTTTGGTGCGAACGCCATTCTGGGGGTGTCCCTTGCCGTCTGCAAA
GCTGGTGCCGTTGAGAAGGGGGTCCCCCTGTACCGCCACATCGCTGACTTGGCTGGCAAC
TCTGAAGTCATCCTGCCAGTCCCGGCGTTCAATGTCATCAATGGCGGTTCTCATGCTGGC
AACAAGCTGGCCATGCAGGAGTTCATGATCCTCCCAGTCGGTGCAGCAAACTTCAGGGAA
GCCATGCGCATTGGAGCAGAGGTTTACCACAACCTGAAGAATGTCATCAAGGAGAAATAT
GGGAAAGATGCCACCAATGTGGGGGATGAAGGCGGGTTTGCTCCCAACATCCTGGAGAAT
AAAGAAGGCCTGGAGCTGCTGAAGACTGCTATTGGGAAAGCTGGCTACACTGATAAGGTG
GTCATCGGCATGGACGTAGCGGCCTCCGAGTTCTTCAGGTCTGGGAAGTATGACCTGGAC
TTCAAGTCTCCCGATGACCCCAGCAGGTACATCTCGCCTGACCAGCTGGCTGACCTGTAC
AAGTCCTTCATCAAGGACTACCCAGTGGTGTCTATCGAAGATCCCTTTGACCAGGATGAC
TGGGGAGCTTGGCAGAAGTTCACAGCCAGTGCAGGAATCCAGGTAGTGGGGGATGATCTC
ACAGTGACCAACCCAAAGAGGATCGCCAAGGCCGTGAACGAGAAGTCCTGCAACTGCCTC
CTGCTCAAAGTCAACCAGATTGGCTCCGTGACCGAGTCTCTTCAGGCGTGCAAGCTGGCC
CAGGCCAATGGTTGGGGCGTCATGGTGTCTCATCGTTCGGGGGAGACTGAAGATACCTTC
ATCGCTGACCTGGTTGTGGGGCTGTGCACTGGGCAGATCAAGACTGGTGCCCCTTGCCGA
TCTGAGCGCTTGGCCAAGTACAACCAGCTCCTCAGAATTGAAGAGGAGCTGGGCAGCAAG
GCTAAGTTTGCCGGCAGGAACTTCAGAAACCCCTTGGCCAAGTAA
Enzyme 5 GenBank Gene ID M14328 Link Image
Enzyme 5 GeneCard ID ENO1 Link Image
Enzyme 5 GenAtlas ID ENO1 Link Image
Enzyme 5 HGNC ID HGNC:3350 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 1p36.3-p36.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Giallongo A, Feo S, Moore R, Croce CM, Showe LC: Molecular cloning and nucleotide sequence of a full-length cDNA for human alpha enolase. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6741-5. [PubMed Link Image]
  2. Giallongo A, Oliva D, Cali L, Barba G, Barbieri G, Feo S: Structure of the human gene for alpha-enolase. Eur J Biochem. 1990 Jul 5;190(3):567-73. [PubMed Link Image]
  3. Ray R, Miller DM: Cloning and characterization of a human c-myc promoter-binding protein. Mol Cell Biol. 1991 Apr;11(4):2154-61. [PubMed Link Image]
  4. Walter M, Berg H, Leidenberger FA, Schweppe KW, Northemann W: Autoreactive epitopes within the human alpha-enolase and their recognition by sera from patients with endometriosis. J Autoimmun. 1995 Dec;8(6):931-45. [PubMed Link Image]
  5. Onyango P, Lubyova B, Gardellin P, Kurzbauer R, Weith A: Molecular cloning and expression analysis of five novel genes in chromosome 1p36. Genomics. 1998 Jun 1;50(2):187-98. [PubMed Link Image]
  6. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [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. Mohammad RM, Hamdan MY, al-Katib A: Induced expression of alpha-enolase in differentiated diffuse large cell lymphoma. Enzyme Protein. 1994-1995;48(1):37-44. [PubMed Link Image]
  9. Ghosh AK, Steele R, Ray RB: Functional domains of c-myc promoter binding protein 1 involved in transcriptional repression and cell growth regulation. Mol Cell Biol. 1999 Apr;19(4):2880-6. [PubMed Link Image]
  10. Feo S, Arcuri D, Piddini E, Passantino R, Giallongo A: ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1). FEBS Lett. 2000 May 4;473(1):47-52. [PubMed Link Image]
  11. Lopez-Alemany R, Longstaff C, Hawley S, Mirshahi M, Fabregas P, Jardi M, Merton E, Miles LA, Felez J: Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against alpha-Enolase. Am J Hematol. 2003 Apr;72(4):234-42. [PubMed Link Image]
  12. Arza B, Felez J, Lopez-Alemany R, Miles LA, Munoz-Canoves P: Identification of an epitope of alpha-enolase (a candidate plasminogen receptor) by phage display. Thromb Haemost. 1997 Sep;78(3):1097-103. [PubMed Link Image]
  13. Adamus G, Amundson D, Seigel GM, Machnicki M: Anti-enolase-alpha autoantibodies in cancer-associated retinopathy: epitope mapping and cytotoxicity on retinal cells. J Autoimmun. 1998 Dec;11(6):671-7. [PubMed Link Image]
  14. Subramanian A, Miller DM: Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene. J Biol Chem. 2000 Feb 25;275(8):5958-65. [PubMed Link Image]
  15. Pancholi V: Multifunctional alpha-enolase: its role in diseases. Cell Mol Life Sci. 2001 Jun;58(7):902-20. [PubMed Link Image]
  16. Ghosh AK, Majumder M, Steele R, White RA, Ray RB: A novel 16-kilodalton cellular protein physically interacts with and antagonizes the functional activity of c-myc promoter-binding protein 1. Mol Cell Biol. 2001 Jan;21(2):655-62. [PubMed Link Image]
  17. Ochi H, Horiuchi I, Araki N, Toda T, Araki T, Sato K, Murai H, Osoegawa M, Yamada T, Okamura K, Ogino T, Mizumoto K, Yamashita H, Saya H, Kira J: Proteomic analysis of human brain identifies alpha-enolase as a novel autoantigen in Hashimoto's encephalopathy. FEBS Lett. 2002 Sep 25;528(1-3):197-202. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 14915
Enzyme 6 Name Phosphoglycerate mutase family member 4 (PGAM3)
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name PGAM4
Enzyme 6 Protein Sequence >Phosphoglycerate mutase family member 4 (PGAM3) 
MAAYKLVLIRHGESTWNLENRFSCWYDADLSPAGHEEAKRGGQALRDAGYEFDICLTSVQ
KRVIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYD
VPPPPMEPDHPFYSNISKDRRYADLTEDQLPSYESPKDTIARALPFWNEEIVPQIKEGKR
VLIAAHGNSLQGIAKHVEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVC
KAIEAVAAQGKAKK
Enzyme 6 Number of Residues 254
Enzyme 6 Molecular Weight 28777
Enzyme 6 Theoretical pI 6.63
Enzyme 6 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase 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 Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 82802763 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q5JPN2 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name Q5JPN2_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >762 bp 
ATGGCCGCCTACAAACTGGTGCTGATCCGGCACGGCGAGAGCACATGGAACCTGGAGAAC
CGCTTCAGCTGCTGGTACGACGCCGATCTGAGCCCGGCGGGCCACGAGGAGGCGAAGCGC
GGCGGGCAGGCGCTACGAGATGCTGGCTATGAGTTTGACATCTGCCTCACCTCAGTGCAG
AAGAGAGTGATCCGGACCCTCTGGACAGTGCTAGATGCCATTGATCAGATGTGGCTGCCA
GTGGTGAGGACTTGGCGCCTCAATGAGCGGCACTATGGGGGTCTAACCGGTCTCAATAAA
GCAGAAACTGCTGCAAAGCATGGTGAGGCCCAGGTGAAGATCTGGAGGCGCTCCTATGAT
GTCCCACCACCTCCGATGGAGCCCGACCATCCTTTCTACAGCAACATCAGTAAGGATCGC
AGGTATGCAGACCTCACAGAAGATCAGCTACCCTCCTATGAGAGTCCGAAGGATACTATT
GCCAGAGCTCTGCCCTTCTGGAATGAAGAAATAGTTCCCCAGATCAAGGAGGGGAAACGT
GTACTGATTGCAGCCCATGGCAACAGCCTCCAGGGCATTGCCAAGCATGTGGAGGGTCTC
TCTGAAGAGGCTATCATGGAGCTGAACCTGCCGACTGGTATTCCCATCGTCTATGAATTG
GACAAGAACTTGAAGCCTATCAAGCCCATGCAGTTTCTGGGGGATGAAGAGACGGTGTGC
AAAGCCATAGAAGCTGTGGCTGCCCAGGGCAAGGCCAAGAAG
Enzyme 6 GenBank Gene ID DQ120647 Link Image
Enzyme 6 GeneCard ID Q5JPN2 Link Image
Enzyme 6 GenAtlas ID PGAM4 Link Image
Enzyme 6 HGNC ID HGNC:21731 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available