ID   PGK_CLOAB               Reviewed;         397 AA.
AC   O52632;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=CA_C0710;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=10463150; DOI=10.1099/13500872-145-8-1839;
RA   Schreiber W., Durre P.;
RT   "The glyceraldehyde-3-phosphate dehydrogenase of Clostridium
RT   acetobutylicum: isolation and purification of the enzyme, and sequencing
RT   and localization of the gap gene within a cluster of other glycolytic
RT   genes.";
RL   Microbiology 145:1839-1847(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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 {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; AF043386; AAC13161.1; -; Genomic_DNA.
DR   EMBL; AE001437; AAK78687.1; -; Genomic_DNA.
DR   PIR; D96987; D96987.
DR   RefSeq; NP_347347.1; NC_003030.1.
DR   RefSeq; WP_010964029.1; NC_003030.1.
DR   AlphaFoldDB; O52632; -.
DR   SMR; O52632; -.
DR   STRING; 272562.CA_C0710; -.
DR   GeneID; 44997221; -.
DR   KEGG; cac:CA_C0710; -.
DR   PATRIC; fig|272562.8.peg.913; -.
DR   eggNOG; COG0126; Bacteria.
DR   HOGENOM; CLU_025427_0_2_9; -.
DR   OrthoDB; 9808460at2; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000000814; Chromosome.
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   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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..397
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145931"
FT   BINDING         23..25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         61..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         353..356
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  42384 MW;  8F1C993B0447966B CRC64;
     MKFNKKTIED VDVKGKRVLV RCDFNVPLKD GVITDENRLN GALPTIKYLS EHGGKVILCS
     HLGKAKGPDP SKTLAPVAKR LSELLGREVK FAADDTVVGE NAKKAVAELK EGEIVLLENT
     RFRPEEGKND DAFSKDLASL ADVYVNDAFG TAHRAHCSTV GVTKFVDTAV CGYLIQKELK
     FLGSAVENPV RPFVAILGGA KVSDKINVIN NLLEKVDTLI IGGGMAYTFL KAQGYTIGTS
     LLEADKVDYA KEMIEKAEAK GVKLLLPIDN IVGAEFKADT KAVTTEDANI PEGYMGLDIG
     PKTQKLYADA VKEAKTVVWN GPMGVFEFEN FAKGTKDVAK AMAESDATTV IGGGDSAAAV
     NQLGFGDKMT HISTGGGASL EFLEGKELPG IVALNDK
//