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Database: UniProt
Entry: A7FNU8
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Original site: A7FNU8 
ID   PCKA_YERP3              Reviewed;         539 AA.
AC   A7FNU8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   29-OCT-2014, entry version 49.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [ATP] {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PCK {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00453};
DE            EC=4.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00453};
GN   Name=pckA {ECO:0000255|HAMAP-Rule:MF_00453};
GN   OrderedLocusNames=YpsIP31758_3978;
OS   Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=349747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP 31758;
RX   PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA   Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA   Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT   "The complete genome sequence of Yersinia pseudotuberculosis IP31758,
RT   the causative agent of Far East scarlet-like fever.";
RL   PLoS Genet. 3:1508-1523(2007).
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the
CC       conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP)
CC       through direct phosphoryl transfer between the nucleoside
CC       triphosphate and OAA. {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- CATALYTIC ACTIVITY: ATP + oxaloacetate = ADP + phosphoenolpyruvate
CC       + CO(2). {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- COFACTOR: Binds 1 manganese ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00453}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [ATP]
CC       family. {ECO:0000255|HAMAP-Rule:MF_00453}.
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DR   EMBL; CP000720; ABS47683.1; -; Genomic_DNA.
DR   RefSeq; YP_001402926.1; NC_009708.1.
DR   ProteinModelPortal; A7FNU8; -.
DR   SMR; A7FNU8; 5-539.
DR   STRING; 349747.YpsIP31758_3978; -.
DR   EnsemblBacteria; ABS47683; ABS47683; YpsIP31758_3978.
DR   GeneID; 5386776; -.
DR   KEGG; ypi:YpsIP31758_3978; -.
DR   PATRIC; 18637277; VBIYerPse15693_4527.
DR   eggNOG; COG1866; -.
DR   HOGENOM; HOG000271471; -.
DR   KO; K01610; -.
DR   OMA; SKTENAR; -.
DR   OrthoDB; EOG6DG2RK; -.
DR   BioCyc; YPSE349747:GH71-4083-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.449.10; -; 1.
DR   Gene3D; 3.90.228.20; -; 2.
DR   HAMAP; MF_00453; PEPCK_ATP; 1.
DR   InterPro; IPR001272; PEP_carboxykinase_ATP.
DR   InterPro; IPR013035; PEP_carboxykinase_C.
DR   InterPro; IPR008210; PEP_carboxykinase_N.
DR   InterPro; IPR015994; PEPCK_ATP_CS.
DR   Pfam; PF01293; PEPCK_ATP; 1.
DR   PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR   SUPFAM; SSF68923; SSF68923; 1.
DR   TIGRFAMs; TIGR00224; pckA; 1.
DR   PROSITE; PS00532; PEPCK_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Decarboxylase;
KW   Gluconeogenesis; Lyase; Manganese; Metal-binding; Nucleotide-binding.
FT   CHAIN         1    539       Phosphoenolpyruvate carboxykinase [ATP].
FT                                /FTId=PRO_1000060310.
FT   NP_BIND     247    255       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   NP_BIND     448    449       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   METAL       212    212       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   METAL       231    231       Manganese; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   METAL       268    268       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING      64     64       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     206    206       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     212    212       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     212    212       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     231    231       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     296    296       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     332    332       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     332    332       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     454    454       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
SQ   SEQUENCE   539 AA;  59337 MW;  D8378DA3417974C4 CRC64;
     MSVKGITPQE LAAYGIHNVS EIVYNPSYDL LFEEETKPTL EGYERGTLTT TGAIAVDTGI
     FTGRSPKDKY IVRDAITQDT VWWADQGKGK NDNKPLSQEI WSHLKGLVTE QLSGKRLFVV
     DTFCGANADT RLQVRFITEV AWQAHFVKNM FIRPSDEELA RFEPDFIVMN GAKCTNPQWK
     EQGLNSENFV AFNLTERMQL IGGTWYGGEM KKGMFSMMNY LLPLKGIASM HCSANVGEKG
     DVAIFFGLSG TGKTTLSTDP KRKLIGDDEH GWDDDGVFNF EGGCYAKTIK LSEEAEPDIY
     HAIKRDALLE NVVVLADGTV DFNDGSKTEN TRVSYPIYHI DNIVKPVSKA GHATKVIFLT
     ADAFGVLPPV SRLTANQTQY HFLSGFTAKL AGTERGVTEP TPTFSACFGA AFLSLHPTQY
     AEVLVKRMQA VGAQAYLVNT GWNGTGKRIS IKDTRAIIDA ILNGEIDKAE TFTLPIFDLA
     VPMSLPGVNP DILDPRDTYA DKAQWQEKAE DLAKRFATNF DKYTDTPAGA ALVSAGPKI
//
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