ID F8C3U2_THEGP Unreviewed; 493 AA. AC F8C3U2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAR-2024, entry version 47. DE SubName: Full=Phosphoenolpyruvate carboxylase {ECO:0000313|EMBL:AEH23660.1}; DE EC=4.1.1.31 {ECO:0000313|EMBL:AEH23660.1}; GN OrderedLocusNames=TOPB45_1582 {ECO:0000313|EMBL:AEH23660.1}; OS Thermodesulfobacterium geofontis (strain OPF15). OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria; OC Thermodesulfobacteriales; Thermodesulfobacteriaceae; OC Thermodesulfobacterium. OX NCBI_TaxID=795359 {ECO:0000313|EMBL:AEH23660.1, ECO:0000313|Proteomes:UP000006583}; RN [1] {ECO:0000313|EMBL:AEH23660.1, ECO:0000313|Proteomes:UP000006583} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OPF15 {ECO:0000313|EMBL:AEH23660.1, RC ECO:0000313|Proteomes:UP000006583}; RX PubMed=23580711; DOI=10.1128/genomea.00162-13; RA Elkins J.G., Hamilton-Brehm S.D., Lucas S., Han J., Lapidus A., Cheng J.F., RA Goodwin L.A., Pitluck S., Peters L., Mikhailova N., Davenport K.W., RA Detter J.C., Han C.S., Tapia R., Land M.L., Hauser L., Kyrpides N.C., RA Ivanova N.N., Pagani I., Bruce D., Woyke T., Cottingham R.W.; RT "Complete genome sequence of the hyperthermophilic sulfate-reducing RT bacterium Thermodesulfobacterium geofontis OPF15T."; RL Genome Announc. 1:E0016213-E0016213(2013). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002829; AEH23660.1; -; Genomic_DNA. DR RefSeq; WP_013910358.1; NC_015682.1. DR AlphaFoldDB; F8C3U2; -. DR STRING; 795359.TOPB45_1582; -. DR KEGG; top:TOPB45_1582; -. DR PATRIC; fig|795359.3.peg.1609; -. DR eggNOG; COG1892; Bacteria. DR HOGENOM; CLU_517433_0_0_0; -. DR OrthoDB; 5487470at2; -. DR Proteomes; UP000006583; Chromosome. DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0015977; P:carbon fixation; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR HAMAP; MF_01904; PEPcase_type2; 1. DR InterPro; IPR007566; PEP_COase_arc-type. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR NCBIfam; TIGR02751; PEPCase_arch; 1. DR Pfam; PF14010; PEPcase_2; 1. DR PIRSF; PIRSF006677; UCP006677; 1. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. PE 3: Inferred from homology; KW Lyase {ECO:0000313|EMBL:AEH23660.1}; KW Pyruvate {ECO:0000313|EMBL:AEH23660.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006583}. SQ SEQUENCE 493 AA; 56924 MW; A97703A432EB4281 CRC64; MKIPRVMSTQ HPDNVSIPFF AEHADMSGED EIQEAYYAFS HLGCDEQMWD SEGKEVDDFV VKKLLSKYPT FFKNKKLGKD VFITLRIPNP TVEKEEAKIL VEALESIPRS MDAAKVFYEN PYPPIFEVIL PMTTSAKELN RVYYFYKNFI SGKQYQKIYE EDITVAEWVG EFLPERINVI PLFEDVETLF NVDKILFEYL KDKDFNYLRV FLARSDPALN YGMISAVLAI KVALKKLEKV AQEKEIEIYP ILGAGTPPFR GNLSPYTVDK VLNEFSPVET FTVQSAFKYD FPIEDVITGI KKLKNFIRYP LEDVDEKFCK KIIEKFSKEY HSLISPLAPA INELAKYVPK RRMRKLHIGL FGYSRSVGGV TLPRVINFCA ACYSIGLPPE LLGVNCLDKE ELKDLKNIYK NLEYDFSIAL QYFNPKCLEL LNEEEKNKII KSLEVLNSLD IKYTVHIEHK EVTTNILKNL KRGITSNLSE LLIEGAYLRK FLG //