PGK_COPPD
ID PGK_COPPD Reviewed; 393 AA.
AC B5Y8I0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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};
GN OrderedLocusNames=COPRO5265_0729;
OS Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / OCM 4 /
OS BT).
OC Bacteria; Coprothermobacterota; Coprothermobacteria; Coprothermobacterales;
OC Coprothermobacteraceae; Coprothermobacter.
OX NCBI_TaxID=309798;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Coprothermobacter proteolyticus strain
RT ATCC 5245 / DSM 5265 / BT.";
RL Submitted (AUG-2008) 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; CP001145; ACI16869.1; -; Genomic_DNA.
DR RefSeq; WP_012543521.1; NC_011295.1.
DR AlphaFoldDB; B5Y8I0; -.
DR SMR; B5Y8I0; -.
DR STRING; 309798.COPRO5265_0729; -.
DR EnsemblBacteria; ACI16869; ACI16869; COPRO5265_0729.
DR KEGG; cpo:COPRO5265_0729; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_9; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 462069at2; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000001732; 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; 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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..393
FT /note="Phosphoglycerate kinase"
FT /id="PRO_1000096334"
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 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 348..351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ SEQUENCE 393 AA; 42974 MW; 409A6BFB60BFEF94 CRC64;
MKLRSIRDAE VRNKRVIVRV DFNVPLDAEG NVVDDFRIRA ALPTIEYLVE NGAKVILISH
LGRPKGKRDK KYSLVGVAKR LAELLHKEIL FAPDVVGEEV ELAVNGLRSG DILLCENVRF
HEEEEKNDAE FAKNIASLGE IFVNDAFSAS HRAHATVEGI TKFLPSYAGF LMEKEVNYLS
MLTENPQRPY YLVLGGAKVS DKVALLQNLL PKVDGMVIGG AMVFTFWKAQ GKEIGKSIVE
DDLVGFAKEL LEQATTQNKE IVLAKDFVVA DENKEHVEIK AISDFGPADI GYDIGPESIK
EFKNALVKAR TVFWNGPLGL FEDAKFAEGT KQVGAFLADF PGTVVVGGGD TANAVREMEL
FEKFAHVSTG GGASLEFLEG KVLPGIAPLV VEG
