ID   PGK_APLCA               Reviewed;         412 AA.
AC   O61471;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=PGK;
OS   Aplysia californica (California sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=6500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10701873; DOI=10.1101/lm.4.6.478;
RA   Zwartjes R.E., West H., Hattar S., Ren X., Noel F., Nunez-Regueiro M.,
RA   Macphee K., Homayouni R., Crow M.T., Byrne J.H., Eskin A.;
RT   "Identification of specific mRNAs affected by treatments producing long-
RT   term facilitation in Aplysia.";
RL   Learn. Memory 4:478-495(1998).
CC   -!- FUNCTION: Catalyzes one of the two ATP producing reactions in the
CC       glycolytic pathway via the reversible conversion of 1,3-
CC       diphosphoglycerate to 3-phosphoglycerate. In addition to its role as a
CC       glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha
CC       cofactor protein (primer recognition protein). May play a role in sperm
CC       motility. {ECO:0000250|UniProtKB:P00558}.
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:0000250|UniProtKB:P00558};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000250|UniProtKB:P00558}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; AF042738; AAC13267.1; -; mRNA.
DR   RefSeq; NP_001191644.1; NM_001204715.1.
DR   AlphaFoldDB; O61471; -.
DR   SMR; O61471; -.
DR   PRIDE; O61471; -.
DR   GeneID; 101859700; -.
DR   UniPathway; UPA00109; UER00185.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; -; 3.
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; PTHR11406; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; SSF53748; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..412
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145842"
FT   BINDING         21..23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         60..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         308
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         339
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
FT   BINDING         368..371
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB7"
SQ   SEQUENCE   412 AA;  43653 MW;  99B63AA7A2CC2D02 CRC64;
     MNKLSINDVD VRDKRVLIRV DFNVPLKNGQ ISNNQRIAAA LPTIKLALEK GAKSVVLMSH
     LGRPDGRPIH AASMKPVVAE LENLLGKKIM FLEDCVGSKV EAACANPEPG SVILLENLRF
     HVEKEGKGKD AQGNKAKADD AAVAAFRASL SKLGDVYVND AFGTAHRAHS SMVGVDLPVK
     ACGLLMKKEL DYFAKALENP ARPFLAILGG AKVADKIQLI ENLMDKVNEM IIGGGMAFTF
     LKVLNNMDIG GSLFDEGAKI VGRLVDKAKE KGVKLHLPSD FITGDKFADV AKSATASVAS
     GIPEGWMGLD VGTKTNEVFQ KVIEGAKTIV WNGPPGVFEF ENFSTGSKQM MDSVVRATEA
     GTITIIGGCD TATCAKNSNA TEKVSHVSTG SGTSLELLEG KILPGVAALS QP