(data stored in ACNUC7421 zone)

SWISSPROT: PGK_LEGPC

ID   PGK_LEGPC               Reviewed;         396 AA.
AC   A5I9V7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 75.
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=LPC_0158;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) 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}.
DR   EMBL; CP000675; ABQ54157.1; -; Genomic_DNA.
DR   RefSeq; WP_011945333.1; NC_009494.2.
DR   SMR; A5I9V7; -.
DR   EnsemblBacteria; ABQ54157; ABQ54157; LPC_0158.
DR   KEGG; lpc:LPC_0158; -.
DR   HOGENOM; HOG000227107; -.
DR   KO; K00927; -.
DR   OMA; DMIFDIG; -.
DR   BioCyc; LPNE400673:LPC_RS00735-MONOMER; -.
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;
DR   PRODOM; A5I9V7.
DR   SWISS-2DPAGE; A5I9V7.
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..396
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_1000058006"
FT   NP_BIND         345..348
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   REGION          21..23
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   REGION          59..62
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         36
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         113
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         146
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         197
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         319
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ   SEQUENCE   396 AA;  42551 MW;  FCB13061B14698B4 CRC64;
     MNLIKMSDID LSGKRVLIRE DLNVPIKDGM ITSDQRLQAA LPTIKSALDS GAAVIVLSHL
     GRPEEGKYEK KFSLEPVADY LRENLEYPVR FVKDYLTGVD VNPGELVVCE NVRFNPGEKG
     NDEALAKKLA SLCDVFVMDA FGTAHRAQAS TYGVAQYAPV AVAGPLLIRE LEALNQVLKA
     PKKPIVAIVG GAKVSSKLSL LKQLVGMVDV LIPGGGIANT FLKAQGFEIG ISLYEPDLLD
     EARHILILAK EKGCQIPLPT DVVVGKTFSE TCPAFNKSLS NVAADDMILD IGPETIRDYV
     DLIHEANTII WNGPVGVFEF PQFAYGTRAI AIAIAESDAF SIAGGGDTLA AVDLYDLNQQ
     ISYISTGGGA FLECLEGKTL PAVAILQERA KHVKTN
//

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