ID E3GXT0_METFV Unreviewed; 485 AA. AC E3GXT0; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAR-2024, entry version 53. DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_01904}; DE Short=PEPC {ECO:0000256|HAMAP-Rule:MF_01904}; DE Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_01904}; DE EC=4.1.1.31 {ECO:0000256|HAMAP-Rule:MF_01904}; GN Name=ppcA {ECO:0000256|HAMAP-Rule:MF_01904}; GN OrderedLocusNames=Mfer_0309 {ECO:0000313|EMBL:ADP77112.1}; OS Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S). OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanothermaceae; Methanothermus. OX NCBI_TaxID=523846 {ECO:0000313|EMBL:ADP77112.1, ECO:0000313|Proteomes:UP000002315}; RN [1] {ECO:0000313|EMBL:ADP77112.1, ECO:0000313|Proteomes:UP000002315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S RC {ECO:0000313|Proteomes:UP000002315}; RX PubMed=21304736; RA Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S., RA Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C., RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., RA Mikhailova N., Pati A., Brambilla E., Chen A., Palaniappan K., Land M., RA Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M., RA Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., RA Kyrpides N.C.; RT "Complete genome sequence of Methanothermus fervidus type strain (V24S)."; RL Stand. Genomic Sci. 3:315-324(2010). CC -!- FUNCTION: Catalyzes the irreversible beta-carboxylation of CC phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon CC dicarboxylic acid source for the tricarboxylic acid cycle. CC {ECO:0000256|HAMAP-Rule:MF_01904}. CC -!- CATALYTIC ACTIVITY: CC Reaction=oxaloacetate + phosphate = hydrogencarbonate + CC phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452, CC ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01904}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01904}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01904}. CC -!- SIMILARITY: Belongs to the PEPCase type 2 family. {ECO:0000256|HAMAP- CC Rule:MF_01904}. 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; CP002278; ADP77112.1; -; Genomic_DNA. DR RefSeq; WP_013413390.1; NC_014658.1. DR AlphaFoldDB; E3GXT0; -. DR STRING; 523846.Mfer_0309; -. DR GeneID; 9962024; -. DR KEGG; mfv:Mfer_0309; -. DR HOGENOM; CLU_517433_0_0_2; -. DR OrthoDB; 85849at2157; -. DR Proteomes; UP000002315; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule. DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule. 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 Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01904}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01904, ECO:0000313|EMBL:ADP77112.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01904}; KW Pyruvate {ECO:0000313|EMBL:ADP77112.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002315}. SQ SEQUENCE 485 AA; 56175 MW; A9E6280A83D9BAE0 CRC64; MYIPRCMSTQ HPDNVNPPFF SPNSEIKGED EVTETYYVFS HLGCDEQMWD CEGKEVDNYV VKKLLTKYEL FFRENKLGKD VFLTLRVPNP AIERAESKIL IETLESIPRS YDTAKVFYGE DIAPIFEVIL PMTTSANDLN RIYYYYKKFV AGKEKMLIRK KDITVKEWIG SFKPKEINVI PLFEDYKSML NSDKITENYL RDKNFEYQRV FLARSDPAMN YGMISALLLN KIALMKLDEL AEKISIDIYP IIGIGSAPFR GNLKPKTVDQ IIAEYPSVHT FTIQSSFKYD NPPSDVSKAI KKLKSKKKKN ADIVDIEKSL DIINKYTEQY QKQITNVASI INRLSRFVPS RRKRKLHIGL FGYSRKMGNI VLPRAITFTC VLYSIGVPPE ILGFDALSEK DIDFLSDIYV NFEKDFYDAL KYLDWESPLI TDSLKKSVRE HFPEVEEDRK HVNISRKIYH LLATDGTDSI KESILEAANL RKFLG //