(data stored in ACNUC9543 zone)

SWISSPROT: PGK_YERPA

ID   PGK_YERPA               Reviewed;         387 AA.
AC   Q1CB61;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   08-MAY-2019, entry version 79.
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=YPA_0343;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phospho-D-glycerate + ATP = 3-phospho-D-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216;
CC         EC=2.7.2.3; 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}.
DR   EMBL; CP000308; ABG12311.1; -; Genomic_DNA.
DR   RefSeq; WP_002209963.1; NZ_CP009906.1.
DR   SMR; Q1CB61; -.
DR   PRIDE; Q1CB61; -.
DR   EnsemblBacteria; ABG12311; ABG12311; YPA_0343.
DR   KEGG; ypa:YPA_0343; -.
DR   HOGENOM; HOG000227107; -.
DR   KO; K00927; -.
DR   OMA; DMIFDIG; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000001971; 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;
DR   PRODOM; Q1CB61.
DR   SWISS-2DPAGE; Q1CB61.
KW   ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    387       Phosphoglycerate kinase.
FT                                /FTId=PRO_1000058097.
FT   NP_BIND     340    343       ATP. {ECO:0000255|HAMAP-Rule:MF_00145}.
FT   REGION       21     23       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00145}.
FT   REGION       59     62       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00145}.
FT   BINDING      36     36       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00145}.
FT   BINDING     113    113       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00145}.
FT   BINDING     146    146       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00145}.
FT   BINDING     197    197       ATP. {ECO:0000255|HAMAP-Rule:MF_00145}.
FT   BINDING     314    314       ATP. {ECO:0000255|HAMAP-Rule:MF_00145}.
SQ   SEQUENCE   387 AA;  41074 MW;  B71E0BCD711C7A5D CRC64;
     MSVIKMTDLD LAGKRVLIRA DLNVPVKEGK VTSDARIRAS LPTIEAALKQ GAKVMVTSHL
     GRPTEGEYNE EFSLLPVVNY LKEKLSSPVR LAKDYLDGVE IAAGELVVLE NVRFNKGEKK
     DDEALSKKYA ALCDVYVMDA FGTAHRAQAS THGVGKFAPI ACAGPLLSAE LEALGKALGN
     PARPMVAIVG GSKVSTKLTV LGALSKIADK LIVGGGIANT FVAAQGHNVG KSLYEADLIP
     EAKRLLETCD IPVPTDVRVA TEFSETAAAT LKPANEIKDD EQILDLGDES AERLAEILKN
     AKTILWNGPV GVFEFPNFRK GTEIVARAIA ESEAFSIAGG GDTLAAIDLF GIADQISYIS
     TGGGAFLEFV EGKKLPAVVM LEERAKQ
//

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