PGK_CHLPM
ID PGK_CHLPM Reviewed; 397 AA.
AC A4SH15;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Cvib_1766;
OS Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris
OS vibrioformis (strain DSM 265)).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 265 / 1930;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J.,
RA Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J.,
RA Schuster S.C., Bryant D.A., Richardson P.;
RT "Complete sequence of Prosthecochloris vibrioformis DSM 265.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000607; ABP37774.1; -; Genomic_DNA.
DR RefSeq; WP_011890996.1; NC_009337.1.
DR AlphaFoldDB; A4SH15; -.
DR SMR; A4SH15; -.
DR STRING; 290318.Cvib_1766; -.
DR PRIDE; A4SH15; -.
DR EnsemblBacteria; ABP37774; ABP37774; Cvib_1766.
DR KEGG; pvi:Cvib_1766; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_10; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 462069at2; -.
DR UniPathway; UPA00109; UER00185.
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 CDD; cd00318; Phosphoglycerate_kinase; 1.
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 Transferase.
FT CHAIN 1..397
FT /note="Phosphoglycerate kinase"
FT /id="PRO_1000076598"
FT BINDING 21..23
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 60..63
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 354..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ SEQUENCE 397 AA; 42406 MW; F3B5B684AD5A1F6C CRC64;
MQKKTLSDIT IQGKRILMRV DFNVPLNDER EITDDKRIVE ALPSIRKILD NGGRLILMSH
LGRPKGKVNP IFSLAPVAAK LSELIDTPVA MAEDCIGTEV MQSALALQDG EVMLLENLRF
HPEEEANDPE FAKELAALGE MYVNDAFGTA HRAHASTEGI THFVPTAVAG YLIEKELMYL
GKALEKPERP FVAILGGSKI SGKIDVLENL FKKVDTVLIG GAMVFTFFKA MGLETGSSLV
EDNKLELALS LLEQAKNRNI KLLLPQDVIA APELSADAPF HAVSVKELEA GEMGLDIGPL
TIEAYRQEIL GARTILWNGP MGVFEIDSFA NGTFAVAEAM ALATAKGATT IIGGGDSAAA
VAKAGLASKM THISTGGGAS LEFLEGKELP GIAALND
