ID PCKA2_SALRD Reviewed; 530 AA. AC Q2S008; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=Phosphoenolpyruvate carboxykinase [ATP] 2; DE Short=PEP carboxykinase 2; DE Short=PEPCK; DE EC=4.1.1.49; DE AltName: Full=Phosphoenolpyruvate carboxylase 2; GN Name=pckA2; OrderedLocusNames=SRU_2373; OS Salinibacter ruber (strain DSM 13855). OC Bacteria; Bacteroidetes; Sphingobacteria; Sphingobacteriales; OC Rhodothermaceae; Salinibacter. OX NCBI_TaxID=309807; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16330755; DOI=10.1073/pnas.0509073102; RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., RA Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., RA Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., RA Charlebois R.L., Legault B., Rodriguez-Valera F.; RT "The genome of Salinibacter ruber: convergence and gene exchange among RT hyperhalophilic bacteria and archaea."; RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005). CC -!- CATALYTIC ACTIVITY: ATP + oxaloacetate = ADP + phosphoenolpyruvate CC + CO(2). CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [ATP] CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000159; ABC44838.1; -; Genomic_DNA. DR RefSeq; YP_446473.1; -. DR GeneID; 3852121; -. DR GenomeReviews; CP000159_GR; SRU_2373. DR KEGG; sru:SRU_2373; -. DR NMPDR; fig|309807.5.peg.2245; -. DR TIGR; SRU_2373; -. DR HOGENOM; Q2S008; -. DR OMA; Q2S008; MFIRPTE. DR BioCyc; SRUB309807:SRU_2373-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) act...; IEA:HAMAP. DR GO; GO:0006094; P:gluconeogenesis; IEA:HAMAP. DR HAMAP; MF_00453; -; 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 Gene3D; G3DSA:3.90.228.20; PEP_carboxykinase_C; 1. DR Gene3D; G3DSA:3.40.449.10; PEP_carboxykinase_N; 1. DR Pfam; PF01293; PEPCK_ATP; 1. DR PIRSF; PIRSF006294; PEP_crbxkin; 1. DR ProDom; PD004738; PEPCK_N; 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; Nucleotide-binding. FT CHAIN 1 530 Phosphoenolpyruvate carboxykinase [ATP] FT 2. FT /FTId=PRO_0000236939. FT NP_BIND 232 239 ATP (By similarity). SQ SEQUENCE 530 AA; 59057 MW; 094AEDCD6E1F719B CRC64; MSDLDLSQYG ITPDTTLRNA DPARLYEEAI HYDPTAAIAH SGALTIRSGE KTGRSPADKR IVRHPNSEDD IWWGPINMEI DDHTFEINKE RAQDYLNTRQ RIYVMDGFAG WDPAHRLKVR IICSRPYHAL FMHNMLIRPS QEELASFGEP DFVIYNAGEF PANRQTKHMS SKTSVDLSFE NQEMVILGTE YAGEMKKGVF TVMHYLMPKK DVLSMHCSAN EGDEGDVSLF FGLSGTGKTT LSADPNRKLI GDDEHCWSDD GVFNIEGGCY AKAVGLSEEE EPEIYNAIRY GTVLENMVYD EDTRAVDYDD TSITQNTRAS YPLDYIDRAK IPGMGGHPDN IIFLTYDAFG VMPPVSKLTP EQAMYHFISG YTAKVAGTEV GVDEPQATFS ACFGAAFLVW PPDKYAEMLA EKIRAHDAEA WLVNTGITGG PYGVGHRVPL EHTRAMIDAI HDGSLLDAPK KTEPVFGLDV PTECPNVPND ILMPRETWDD PQAYDEKAEH LVGLFHDHFE KYEDEAAPAI AEAGPQLQAA //