ID A0A1D8T4V0_9NOCA Unreviewed; 918 AA.
AC A0A1D8T4V0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 ORFNames=BFN03_07450 {ECO:0000313|EMBL:AOW92587.1};
OS Rhodococcus sp. WMMA185.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=679318 {ECO:0000313|EMBL:AOW92587.1, ECO:0000313|Proteomes:UP000178767};
RN [1] {ECO:0000313|EMBL:AOW92587.1, ECO:0000313|Proteomes:UP000178767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMMA185 {ECO:0000313|EMBL:AOW92587.1,
RC ECO:0000313|Proteomes:UP000178767};
RA Bugni T.S., Adnani N., Braun D., Chevrette M., McDonald B., Rajski S.;
RT "Draft Genome of Rhodococcus sp. WMMA185.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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,
CC ECO:0000256|HAMAP-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; CP017014; AOW92587.1; -; Genomic_DNA.
DR RefSeq; WP_070378486.1; NZ_CP017014.1.
DR AlphaFoldDB; A0A1D8T4V0; -.
DR STRING; 679318.BFN03_07450; -.
DR KEGG; rhw:BFN03_07450; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000178767; 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 Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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};
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:AOW92587.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000178767}.
FT ACT_SITE 145
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 580
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 918 AA; 100718 MW; 01F428422C54E9F5 CRC64;
MIETPREATE PLREDIRLLG GILGQIVREQ AGDRVFDLVE QARVESFRVR RSEIDRTDLA
EMFARVSSED AIPVIRAFSH FALLANLAED IHRERRRAVH VAAGEPAPDS TLAATYAKLD
AAHLDSALVA AALDGALVSP VITAHPTETR RRTVFETQTR ITDLMRYRER TALTASETAD
VEVRLGRQIL TLWQTALIRL SRLRIQDEIG VGLRYYDAAL FEVVPKINAE LRHALRARWP
DAGLLREPIL RPGSWIGGDR DGNPYVTAEV VRHATTRAAE AAIEHHLGQL VNLEKELSMS
ARLVEVTPAL DLLAAAARDD SPSRVDEPYR RAIRGIRGRL TATAERILGE IPDGGLDSGL
EPYETPREML DELGIVDESL RCSGDAAIAD DGLAALRDSV EVFGFHLSGL DMRQNSEVHE
TVVAEMLAWA GVHEDYRSLS EDERIELLSA ELSSRRPLTT AKAEFSELTA KELAILAAAA
DAVRSIGANA VPNYIISMCT SVSDMLEAAI LLKEAGLFDP GSGESPSCPV GIVPLFETIE
DLQQGAATLE ATLQVPVYRA LVASRGDSQE VMLGYSDSNK DGGYLAANWA LYRAELDLVE
TARKTGIRLR LFHGRGGTVG RGGGPSYDAI LAQPPGAVSG SLRITEQGEV IAAKYAEPPL
AQRNLETLLA ATLEATLLDV EGLGDDAEPA YAILDELATL ARRAYSELVH ETPGFVQYFE
MSTPVAEIGS LNIGSRPASR KQTKEISDLR AIPWVLSWSQ SRVMLPGWYG TGTALEQWTA
RDPGNVATLS RLYQTWPFFR TVLSNMAMVM AKSDMGLAAR YAELVPDEEL RGRVFGKIAD
EHARTIRMYK TITGNDTLFA DNPGLERSLH NRFPYLEPLN HLQVELLRRY RSGDDSDQTR
RGIQLTMNGL ATALRNSG
//