ID PCKA1_SALRD Reviewed; 535 AA. AC Q2S1I3; 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] 1; DE Short=PEP carboxykinase 1; DE Short=PEPCK; DE EC=4.1.1.49; DE AltName: Full=Phosphoenolpyruvate carboxylase 1; GN Name=pckA1; OrderedLocusNames=SRU_1835; 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; ABC44749.1; -; Genomic_DNA. DR RefSeq; YP_445948.1; -. DR GeneID; 3851043; -. DR GenomeReviews; CP000159_GR; SRU_1835. DR KEGG; sru:SRU_1835; -. DR NMPDR; fig|309807.5.peg.1734; -. DR TIGR; SRU_1835; -. DR HOGENOM; Q2S1I3; -. DR OMA; Q2S1I3; ELAWHSL. DR BioCyc; SRUB309807:SRU_1835-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 1 535 Phosphoenolpyruvate carboxykinase [ATP] FT 1. FT /FTId=PRO_0000236938. FT NP_BIND 234 241 ATP (By similarity). SQ SEQUENCE 535 AA; 58886 MW; EBB75A3AB2C54126 CRC64; MPLPNHVTSH LRSLQLAPAA VHYNLKRPRL YEEALDRNEG QLAAGGPLVT RTAPYTGRSP KDRFIVRDAS VADQINWGEV NQPTDRATFD HLHERMAEHA EGRDLFVQDL HAGWDESYRL PVRIITEKAW HSLFARNMFV RPDGPVPDSF EPGFTVVDLC EFEADPERDG THSEAAVFVD IAQNLILIGG THYGGEIKKS IFSVLNYMLP EEGVLPMHCS ANEGEDGDTA VFFGLSGTGK TTLSADASRT LIGDDEHGWS DRGVYNFEGG CYAKMIDITP ESEPEIHGTT EEFGTILENV IVDPDTREPD FSDDTITQNT RGSYPLHYIP NTSSDGRGGH PDHVLFLTYD AFGVLPPVSE LSPAQAMYHF LSGYTAKVAG TEAGVNEPKA TFSTCFGEPF MVRDPSVYAE LLGQKIRRHD TDCWLVNTGM TGGPYGVGHR IELDHTRAMV DAILDGTLGT VARTRDPVFG LSIPDRVPGV PDSVLTPRQT WGDPQAYDQH ARELVDAFAD NFETYVEQVG TEVRAAGPSL ETIRG //