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Database: UniProt/TrEMBL
Entry: Q0S0J1_RHOJR
LinkDB: Q0S0J1_RHOJR
Original site: Q0S0J1_RHOJR 
ID   Q0S0J1_RHOJR            Unreviewed;       918 AA.
AC   Q0S0J1;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   28-MAR-2018, entry version 90.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:ABG98945.1};
GN   OrderedLocusNames=RHA1_ro07181 {ECO:0000313|EMBL:ABG98945.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG98945.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595, ECO:0000256|SAAS:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946753}.
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DR   EMBL; CP000431; ABG98945.1; -; Genomic_DNA.
DR   RefSeq; WP_011598878.1; NC_008268.1.
DR   ProteinModelPortal; Q0S0J1; -.
DR   STRING; 101510.RHA1_ro07181; -.
DR   PRIDE; Q0S0J1; -.
DR   EnsemblBacteria; ABG98945; ABG98945; RHA1_ro07181.
DR   GeneID; 4224731; -.
DR   KEGG; rha:RHA1_ro07181; -.
DR   PATRIC; fig|101510.16.peg.7235; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   BioCyc; RJOS101510:G1G71-7150-MONOMER; -.
DR   Proteomes; UP000008710; 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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008710};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ABG98945.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ABG98945.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   ACT_SITE    145    145       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    580    580       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   918 AA;  101056 MW;  5B70D86784D0BD7F CRC64;
     MIETPREATE PLREDIRLLG GILGQIVREQ AGDSVFDLVE KARVESFRVR RSEIDRADLA
     DMFTQVSTSD TIPVIRAFSH FALLANLAED IHRERRRAVH VAAGEPAPDS TLTATFAKLD
     AAHLDSAVVA DALRGALVSP VITAHPTETR RRTVFETQSR ITELMRYRER TALTESETAD
     VDVRLRRQIL TLWQTALIRL SRLRIQDEIE VGLRYYDAAL FEVVPKINAE LRGALRSRWP
     DADLGREPIL RPGSWIGGDR DGNPYVTDEV VRQATTRAAA TALEHHLGEL ETLERELSMS
     ARLVTVTPAL DLLAAASQDD SPFRADEPYR RAIRGIRGRL TATAHRILGE APDHGLDLGL
     APYDTPRQML DELDVVDDSL RRGGDGTIAD DGLANLRDSV EVFGFHLSGL DMRQNSDVHE
     TVVAELLAWA GVHPDYPSLS EDERVELLSA ELSTRRPLTT ANAEFSELTA KELAILQAGA
     EAVRTLGAGA VPNYIISMCT SVSDMLEAAV LLKEVGLLDP GSGEAPSCPV GIVPLFETIE
     DLQQGAATLE ATLEVPIYRA LVTSRGDSQE VMLGYSDSNK DGGYLAANWA LYRAELDLVD
     AARKTGIRLR LFHGRGGTVG RGGGPSYEAI LAQPPGAVAG SLRITEQGEV IAAKYAEPRL
     AQRNLETLLA ATLEATLLDV EGLGDDAEPA YRILDELAAL ARRAYGELVH ETPGFVEYFE
     MSTPVAEIGA LNIGSRPASR KQTTSISDLR AIPWVLSWSQ SRVMLPGWYG TGAAFEEWTQ
     GDPQRVATLS RLYEKWPFFR TVLSNLAMVM SKSDMGLAAR YAELVPDEEL RRRVFGKIAE
     EHERTIRMYK AITGNDTLFA DNPGLERSVH NRFPYLEPLN HLQVELLRRY RAGDDSDQTR
     RGIQLTMNGL ATALRNSG
//
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