PGK_CAUVN
ID PGK_CAUVN Reviewed; 396 AA.
AC B8H4J9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00145};
DE EC=2.7.2.3 {ECO:0000255|HAMAP-Rule:MF_00145};
GN Name=pgk {ECO:0000255|HAMAP-Rule:MF_00145}; OrderedLocusNames=CCNA_03359;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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:0000255|HAMAP-Rule:MF_00145};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000255|HAMAP-
CC Rule:MF_00145}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00145}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00145}.
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DR EMBL; CP001340; ACL96823.1; -; Genomic_DNA.
DR RefSeq; WP_010921082.1; NC_011916.1.
DR RefSeq; YP_002518731.1; NC_011916.1.
DR AlphaFoldDB; B8H4J9; -.
DR SMR; B8H4J9; -.
DR PRIDE; B8H4J9; -.
DR EnsemblBacteria; ACL96823; ACL96823; CCNA_03359.
DR GeneID; 7332032; -.
DR KEGG; ccs:CCNA_03359; -.
DR PATRIC; fig|565050.3.peg.3272; -.
DR HOGENOM; CLU_025427_0_2_5; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 462069at2; -.
DR PhylomeDB; B8H4J9; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000001364; 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 Gene3D; 3.40.50.1260; -; 2.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
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.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..396
FT /note="Phosphoglycerate kinase"
FT /id="PRO_1000192813"
FT BINDING 21..23
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 59..62
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 353..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ SEQUENCE 396 AA; 40687 MW; 1D81FE9762E9A0C8 CRC64;
MTFRTLDTAD LAGKRALVRV DFNVPVDGGK VADDTRLKAA LPTIRFLADK GAKVVLLAHF
DRPKGKVVPE MSLAFVAEPL AALLGAPVAF VGDCVGPAAA EVVNGLADGG VALLENVRFH
AGEEKNDAEF AKALAANGDV YVNDAFSAAH RAHASTEGLA KLLPAYPGVS MQRELEALDA
ALGNPKKPVI GIVGGSKVST KLDLLNNLVA KLDRLAIGGG MANTFLFAQG HDVGGSLCEK
DLADTAREIM EKAKAAGCEL LLPVDVVVAK KVAPGVETAV RSLSEVQADD LILDAGPESA
KRLLAAMDQS LTLIWNGPLG VFEVPPFDEA TVSAAKHAAS LAKSGKIVAV AGGGDTVAAL
NHAGVSADFT FVSTAGGAFL EWMEGKTLPG VAALES