ID E8PJQ9_THESS Unreviewed; 861 AA. AC E8PJQ9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 24-JAN-2024, entry version 64. DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595}; DE Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595}; DE Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595}; DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595}; GN Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595, GN ECO:0000313|EMBL:ADW22014.1}; GN OrderedLocusNames=TSC_c13950 {ECO:0000313|EMBL:ADW22014.1}; OS Thermus scotoductus (strain ATCC 700910 / SA-01). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=743525 {ECO:0000313|EMBL:ADW22014.1, ECO:0000313|Proteomes:UP000008087}; RN [1] {ECO:0000313|Proteomes:UP000008087} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087}; RA Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R., RA Gottschalk G., van Heerden E., Litthauer D.; RT "The genome sequence of Thermus scotoductus SA-01."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADW22014.1, ECO:0000313|Proteomes:UP000008087} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087}; RX PubMed=22115438; DOI=10.1186/1471-2164-12-577; RA Gounder K., Brzuszkiewicz E., Liesegang H., Wollherr A., Daniel R., RA Gottschalk G., Reva O., Kumwenda B., Srivastava M., Bricio C., RA Berenguer J., van Heerden E., Litthauer D.; RT "Sequence of the hyperplastic genome of the naturally competent Thermus RT scotoductus SA-01."; RL BMC Genomics 12:577-577(2011). CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source CC for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670, CC ECO:0000256|HAMAP-Rule:MF_00595}. 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|ARBA:ARBA00001071, ECO:0000256|HAMAP- CC Rule:MF_00595}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP- CC Rule:MF_00595}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}. CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. CC {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}. 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; CP001962; ADW22014.1; -; Genomic_DNA. DR AlphaFoldDB; E8PJQ9; -. DR STRING; 743525.TSC_c13950; -. DR KEGG; tsc:TSC_c13950; -. DR eggNOG; COG2352; Bacteria. DR HOGENOM; CLU_006557_2_0_0; -. DR Proteomes; UP000008087; 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_00595; PEPcase_type1; 1. DR InterPro; IPR021135; PEP_COase. DR InterPro; IPR022805; PEP_COase_bac/pln-type. DR InterPro; IPR018129; PEP_COase_Lys_AS. DR InterPro; IPR033129; PEPCASE_His_AS. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1. DR PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1. DR Pfam; PF00311; PEPcase; 1. DR PRINTS; PR00150; PEPCARBXLASE. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. DR PROSITE; PS00781; PEPCASE_1; 1. DR PROSITE; PS00393; PEPCASE_2; 1. PE 3: Inferred from homology; KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP- KW Rule:MF_00595}; Coiled coil {ECO:0000256|SAM:Coils}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595}; KW Pyruvate {ECO:0000313|EMBL:ADW22014.1}. FT COILED 154..181 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 148 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10111" FT ACT_SITE 534 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10112" SQ SEQUENCE 861 AA; 96837 MW; 01C5154A961CD6C6 CRC64; MKPAKEDTFD LLRAEVDLLG RLLGEAIRAV SGERFFALVE EVRLLSKARR QGDEGARATL LKRVEGLSLE EAEALVRAFT HYFHLVNLAE ERHRVRVNRL RAQAETPESP RPEGFLALAR ALKERGLSLE EVEAHLNRLE LWLTFTAHPT ETRRRTLRHH LEKLQEELEA QDRSRLAARV ALLYATEEVR KARPTVEDEI KGGLYYLPTT LWQAVPRVVE GLEAALEKVY GRRPRLKSPV RFRSWIGGDR DGNPFVTPEV TAFAARYARQ VARERFLLEL ENLVRDLSLS ETKVPVPRGV REGGEGTERF PGEPYRRFFA RLYTRLEKGE ASTEELLRAL RVAEEGLASV GLEQVAASFL RPLEARLFAF GLELAPLDLR EESGKLLEAA AELLRVGGGH PDFLSLPPEA QEALLTEELR SARPLLPVGH EPQGEALRVA LGAFRAWRDK GAHVVSMTHH PGDLLAVFLL AREVGLYRPG APLPLDVVPL FETLEDLHRA PEVLTRLLQN PVFLAHARGR GGVEIMIGYS DSNKDAGFLA ANLALYEAQE ALAKVGQSFG LPVFFFHGRG TSTARGGGPA GRAIASLPPR SVGHRIRLTE QGEALADRYS HPELAVRHLE QLLFHFAQAA LGEGVEPRPE WREALWQAGE ESMRRYRALL AQEGFFPFFE AFTPIREIGE LPIASRPVYR HGRVREIRDL RAIPWVMAWT QVRLLLPGWY GLTALEALPL DLLRRMYREW PFFATTLENA AMALAKADLG VAELYLRLVP EKLHSLFHGL AQEYQKTVTL LESIFQAPLL HNQRTLERQI ALRNPYVDPI NFVQVELLRR YRAPGGREDE ALKKALLLSI LGVAAGLRNA G //