PGK_PHOLU
ID PGK_PHOLU Reviewed; 387 AA.
AC Q8GF87;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 82.
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};
OS Photorhabdus luminescens (Xenorhabdus luminescens).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=29488;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=W14;
RX PubMed=12564983; DOI=10.1016/s0966-842x(02)02463-0;
RA Waterfield N.R., Daborn P.J., ffrench-Constant R.H.;
RT "Genomic islands in Photorhabdus.";
RL Trends Microbiol. 10:541-545(2002).
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; AF346500; AAO17214.1; -; Genomic_DNA.
DR RefSeq; WP_036808088.1; NZ_PUWW01000031.1.
DR AlphaFoldDB; Q8GF87; -.
DR SMR; Q8GF87; -.
DR STRING; 29488.KS18_06655; -.
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 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 Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..387
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145982"
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 113
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 340..343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ SEQUENCE 387 AA; 41455 MW; 5432B420A3F6C913 CRC64;
MSVIKMTDLD LAGKRVLIRA DLNVPVKDGK VTSDARIRAS LPTIEAALKQ GAKVMITSHL
GRPIEGEYNE EFSLKPVVDY LKEKLSSSVR LEKEYLEGVE VSEGELVVLE NVRFNKGEKK
DDESLAKKYA SLCDIYVMDA FGTAHRAQAS THGVAKFAPV ACAGPLLFGE LEALGKALDN
PARPMVAIVG GSKVSTKLTV LDTLSKIADQ LIVGGGIANT FVAAEGHNVG RSLYEDDLIP
EAKKLLISCD IPVPTDVRVA TEFSETAEAT LKSSSDIKDD EQILDLGDES AQRLADILKN
AKTILWNGPV GVFEFPNFRQ GTEIVARAIA DSDAFSIAGG GDTLAAIDLF GIADKISYIS
TGGGAFLEFV EGKKLPAVVM LEERAKQ