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Database: UniProt/TrEMBL
Entry: A0A1D8T4V0_9NOCA
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Original site: A0A1D8T4V0_9NOCA 
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}.
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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
//
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