ID Q5ENR8_ISOGA Unreviewed; 436 AA.
AC Q5ENR8;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
OS Isochrysis galbana (Marine planktonic alga).
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Isochrysidaceae; Isochrysis.
OX NCBI_TaxID=37099 {ECO:0000313|EMBL:AAW79325.1};
RN [1] {ECO:0000313|EMBL:AAW79325.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15843030; DOI=10.1016/j.jmb.2005.03.030;
RA Patron N.J., Waller R.F., Archibald J.M., Keeling P.J.;
RT "Complex protein targeting to dinoflagellate plastids.";
RL J. Mol. Biol. 348:1015-1024(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000642,
CC ECO:0000256|RuleBase:RU000532};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|RuleBase:RU000532}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU000696}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000256|ARBA:ARBA00008982, ECO:0000256|RuleBase:RU000532}.
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DR EMBL; AY826864; AAW79325.1; -; mRNA.
DR AlphaFoldDB; Q5ENR8; -.
DR UniPathway; UPA00109; UER00185.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR PANTHER; PTHR11406:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000724-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..436
FT /note="Phosphoglycerate kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030175825"
FT BINDING 60..62
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 98..101
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 392..395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ SEQUENCE 436 AA; 45979 MW; 13BC35563B7A6096 CRC64;
MVARTATLAL ALFGGAEALR IGAAPMRSTS RTCTIEMAKK SVGDLTKADL EGKRVLVRCD
LNVPLDGKTI TDDTRIRASI PTIKYLIDNG AKVLLSSHLG RPKGGPEDKF SLGPVAPRLS
ELLGKEVTMA PDCIGDAVAD CVTKMANGDV LLLENTRFYK EEEKNDPEFA EKLAANADMF
VNDAFGTAHR AHGSTEGVTK FLSPSVAGFL LQKELDYLDG AVSDPKRPFA AIVGGSKVSS
KIGVIESLME KVDKIVIGGG MVFTFLKARG LETGSSLVEE DQLELAKKLE VIAKEKGIDF
ILPTDVIVAD KFAADAATQI VSVDAIPEGW MGLDNGPEST KMIQQKLSEC KTIIWNGPMG
VFEFEAFAKG TFDVADTLAE LTGKGCTTII GGGDSVAAVE KAGLAEKMSH ISTGGGASLE
LLEGKVLPGV AALQEA
//
