(data stored in ACNUC7421 zone)

SWISSPROT: PGK_PSEAB

ID   PGK_PSEAB               Reviewed;         387 AA.
AC   Q02TL3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 64.
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=PA14_07190;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-
CC       D-glyceroyl phosphate. {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; CP000438; ABJ15515.1; -; Genomic_DNA.
DR   RefSeq; WP_003084960.1; NC_008463.1.
DR   ProteinModelPortal; Q02TL3; -.
DR   SMR; Q02TL3; -.
DR   PRIDE; Q02TL3; -.
DR   EnsemblBacteria; ABJ15515; ABJ15515; PA14_07190.
DR   KEGG; pau:PA14_07190; -.
DR   HOGENOM; HOG000227107; -.
DR   KO; K00927; -.
DR   OMA; DMIFDIG; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000000653; 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-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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   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; Q02TL3.
DR   SWISS-2DPAGE; Q02TL3.
KW   ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    387       Phosphoglycerate kinase.
FT                                /FTId=PRO_1000058036.
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;  40405 MW;  3787C6ED28E22C4E CRC64;
     MTVLKMTDLD LKGKRVLIRE DLNVPVKDGQ VQSDARIKAA LPTLKLALEK GAAVMVCSHL
     GRPTEGEFSA ENSLKPVAEY LSKALGREVP LLADYLDGVE VKAGDLVLFE NVRFNKGEKK
     NADELAQKYA ALCDVFVMDA FGTAHRAEGS THGVARFAKV AAAGPLLAAE LDALGKALGN
     PARPMAAIVA GSKVSTKLDV LNSLAGICDQ LIVGGGIANT FLAAAGHKVG KSLYEADLVE
     TAKAIAAKVK VPLPVDVVVA KEFAESAVAT VKAIAEVADD DMILDIGPQT AAQFAELLKT
     SKTILWNGPV GVFEFDQFGE GTRTLANAIA DSAAFSIAGG GDTLAAIDKY GIAERISYIS
     TGGGAFLEFV EGKVLPAVEI LEQRAKG
//

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