| General Information |
| MoonProt ID | 130 |
| First appeared in release | 1.0 |
| Name(s) | Phosphoglycerate kinase 1
Cell migration-inducing gene 10 protein
Primer recognition protein 2
Plasmin Reductase
PGKA
PRP 2
Gene Name: PGK1
|
| UniProt ID | P00558 (PGK1_HUMAN) Reviewed |
| GO terms | GO:0005975 carbohydrate metabolic process
GO:0006006 glucose metabolic process
GO:0006094 gluconeogenesis
GO:0006096 glycolysis
GO:0016310 phosphorylation
GO:0030855 epithelial cell differentiation
GO:0044281 small molecule metabolic process
GO:0000166 nucleotide binding
GO:0004618 phosphoglycerate kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016740 transferase activity
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular vesicular exosome
|
| Organisms for which functions have been demonstrated | Homo sapiens (human, a mammal) |
| Sequence length | 417 |
| FASTA sequence | >gi|4505763|ref|NP_000282.1| phosphoglycerate kinase 1 [Homo sapiens]
MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEPVAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGPESSKKYAEAVTRAKQIVWNGPVGVFEWEAFARGTKALMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNI |
| Structure Information |
| PDB ID | 2WZB 2WZC 2WZD 2X13 2X14 2X15 2XE6 2XE7 2XE8 2Y3I
2YBE 2ZGV 3C39 3C3A 3C3B 3C3C |
| Quaternary structure | |
| SCOP | Phosphoglycerate kinase |
| CATH | 3.40.50.1260 |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 1-7, 131-143, 415-417 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | Phosphoglycerate Kinase, enzyme
ADP + 1,3-bisphosphoglycerate => ATP + 3-phospho-D-glycerate
Carbohydrate degradation, glycolysis |
| References for function | Michelson AM, Markham AF, Orkin SH. Isolation and DNA sequence of a full-length cDNA clone for human X chromosome-encoded phosphoglycerate kinase. Proc Natl Acad Sci U S A. 1983 Jan. PMID: 6188151 |
| E.C. number | 2.7.2.3 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | Subtrate binding site of 1,3-bisphosphoglycerate (bPG): Asp23, Asn25, Arg38, His62, Arg65, Arg122, Arg170. Subtrate Binding site of ADP: Ala214, Lys215, Lys219, Gly312, Asn336, Glu343, Asp374, Thr375.
Reference: Transition State Analogue Structures of Human Phosphoglycerate Kinase Establish the Importance of Charge Balance in Catalysis Matthew J. Cliff, Matthew W. Bowler, Andrea Varga, James P. Marston, Judit Szab, Andrea M. Hounslow, Nicola J. Baxter, G. Michael Blackburn, Mria Vas, and Jonathan P. Waltho. Journal of the American Chemical Society 2010 132 (18), 6507-6516
PubMed ID (20397725) DOI (10.1021/ja100974t) |
| Function 2 |
| Function description | disulphide reductase, enzyme
Inhibits angiogenesis through a disulfide reductase activity that activates plasminogen autoproteolytic activity, producing angiostatin. One or more of the PGK cysteine residues may have a role in plasmin reduction. |
| References for function | Lay AJ, Jiang XM, Kisker O, Flynn E, Underwood A, Condron R, Hogg PJ. Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase. Nature. 2000 Dec 14. PMID: 11130727 |
| E.C. number | N/A |
| Location of functional site(s) | |
| Cellular location of function | Extracellular. Secreted Protein. |
| Comments | |