ID   PGK_VIBC3               Reviewed;         387 AA.
AC   A5F9G2; C3LX30; P96154; Q9KUN8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   24-JAN-2024, entry version 89.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=VC0395_A0030, VC395_0521;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RX   PubMed=8982014; DOI=10.1128/jb.179.1.293-296.1997;
RA   Carroll P.A., Zhao G., Boyko S.A., Winkler M.E., Calderwood S.B.;
RT   "Identification, sequencing, and enzymatic activity of the erythrose-4-
RT   phosphate dehydrogenase gene of Vibrio cholerae.";
RL   J. Bacteriol. 179:293-296(1997).
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   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABQ19963.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=ACP08540.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000627; ABQ19963.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001235; ACP08540.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U72152; AAC44768.1; -; Genomic_DNA.
DR   RefSeq; WP_000111267.1; NZ_JAACZH010000029.1.
DR   AlphaFoldDB; A5F9G2; -.
DR   SMR; A5F9G2; -.
DR   GeneID; 66938812; -.
DR   KEGG; vco:VC0395_A0030; -.
DR   KEGG; vcr:VC395_0521; -.
DR   PATRIC; fig|345073.21.peg.509; -.
DR   eggNOG; COG0126; Bacteria.
DR   HOGENOM; CLU_025427_0_2_6; -.
DR   OrthoDB; 9808460at2; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000000249; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..387
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000324783"
FT   BINDING         21..23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         340..343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   387 AA;  40979 MW;  0D7EBFBF5C93F719 CRC64;
     MSVIKMIDLD LAGKRVFIRA DLNVPVKDGK VTSDARILAS LPTIKHCLEA GAKVMVTSHL
     GRPTEGEYAE EFSLLPVVNY LNDALDCEVR LVKDYLDGVE LNAGELVVLE NVRFNKGEKK
     NEEALSKKYA ALCDVFVMDA FGTAHRAQAS THGVGMFAPI ACAGPLLADE LEALGKAMDK
     PARPMVAIVG GSKVSTKLTV LESLSKIADQ LVVGGGIANT FIAAAGHNVG KSLYEADLVE
     TAKKLMEECA IPVATDVACA KAFDENAEAE IKHVSEVQDD DMIFDLGPNS TAELAEILKN
     AKTILWNGPV GVFEFKNFEA GTRGIAEAIA QSEGFSVAGG GDTLAAIDKF GIKADVSYIS
     TGGGAFLEFV EGKKLPAVEM LEARAKA
//