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Database: UniProt
Entry: A9KDE5
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ID   PCKA_COXBN              Reviewed;         517 AA.
AC   A9KDE5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   01-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=CBUD_2191;
OS   Coxiella burnetii (strain Dugway 5J108-111).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Coxiellaceae; Coxiella.
OX   NCBI_TaxID=434922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dugway 5J108-111;
RX   PubMed=19047403; DOI=10.1128/IAI.01141-08;
RA   Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA   Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F.,
RA   Samuel J.E., Heinzen R.A.;
RT   "Comparative genomics reveal extensive transposon-mediated genomic
RT   plasticity and diversity among potential effector proteins within the
RT   genus Coxiella.";
RL   Infect. Immun. 77:642-656(2009).
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; CP000733; ABS76965.1; -; Genomic_DNA.
DR   RefSeq; WP_011997467.1; NC_009727.1.
DR   RefSeq; YP_001425493.1; NC_009727.1.
DR   ProteinModelPortal; A9KDE5; -.
DR   STRING; 434922.CBUD_2191; -.
DR   EnsemblBacteria; ABS76965; ABS76965; CBUD_2191.
DR   GeneID; 5458505; -.
DR   KEGG; cbd:CBUD_2191; -.
DR   PATRIC; 17924171; VBICoxBur32972_2158.
DR   eggNOG; COG1866; -.
DR   HOGENOM; HOG000271471; -.
DR   KO; K01610; -.
DR   OMA; GADPEHY; -.
DR   OrthoDB; EOG6DG2RK; -.
DR   BioCyc; CBUR434922:GJTP-2300-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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    517       Phosphoenolpyruvate carboxykinase [ATP].
FT                                /FTId=PRO_1000080992.
FT   NP_BIND     221    229       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   METAL       186    186       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   METAL       205    205       Manganese; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   METAL       242    242       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING      46     46       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     180    180       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     186    186       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     186    186       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     205    205       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     270    270       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     306    306       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
FT   BINDING     306    306       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00453}.
FT   BINDING     433    433       ATP. {ECO:0000255|HAMAP-Rule:MF_00453}.
SQ   SEQUENCE   517 AA;  56765 MW;  5AD9A641C1B1A0A3 CRC64;
     MEQIAARVTY INLSPDELIQ HAVKNGEGVL SSTGALAVTT GKRTGRSPKD RFIVKDEQTA
     DQVAWGNINQ PVEQRTFDQL WERALRYLSE RAVYISHLQV GADDNYFLPL KVVTEFAWHN
     LFACDLFIRP SGDHANGKPS WVILSAPGLK TDPERDGVNS DGAVMINLSQ RRVLLVGMPY
     AGEMKKAMFS VLNYLLPPHD VLPMHCAANA GQSGDVALFF GLSGTGKTTL SADPHRFLIG
     DDEHGWSATS VFNFEGGCYA KCIDLSQERE PMIWNAIRHG AIMENVVLDE NGVPDYADAR
     LTQNSRAAYP REHIPLRVEN NRGRPPDAVL FLTCDLDGVL PPVALLTKEQ AAYYFLSGYT
     ALVGSTEVGS VKGVTSTFST CFGAPFFPRP PTVYAELLMK RIEATGCQVY LVNTGWTGGA
     YGEGGERFSI PTTRAIVNAV LSGKLKEGPT EVLSGFNLTI PKSALGVDDH LLNPRKTWED
     VSAYDARAQR LIQKFRENFE KFKVPAAIRE AGPSDVH
//
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