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Database: UniProt/TrEMBL
Entry: C1B4M0_RHOOB
LinkDB: C1B4M0_RHOOB
Original site: C1B4M0_RHOOB 
ID   C1B4M0_RHOOB            Unreviewed;       918 AA.
AC   C1B4M0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   25-APR-2018, entry version 66.
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:BAH55209.1};
GN   OrderedLocusNames=ROP_69620 {ECO:0000313|EMBL:BAH55209.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH55209.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH55209.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH55209.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; AP011115; BAH55209.1; -; Genomic_DNA.
DR   RefSeq; WP_015890634.1; NC_012522.1.
DR   STRING; 632772.ROP_69620; -.
DR   EnsemblBacteria; BAH55209; BAH55209; ROP_69620.
DR   KEGG; rop:ROP_69620; -.
DR   PATRIC; fig|632772.20.peg.7253; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000002212; 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:UP000002212};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:BAH55209.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:BAH55209.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002212}.
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;  100828 MW;  85D8643C9D7B4342 CRC64;
     MIETPREATE PLREDIRLLG GILGQIVREQ AGDGVFDLVE KARVESFRVR RSEIDRAELA
     DMFTEVSTSD AIPVIRAFSH FALLANLAED NHRERRRAVH VAAGEPAPDS TLTATFAKLD
     AAHLGSDVVA DALRGALVSP VITAHPTETR RRTVFETQTR ITELMRYRER TALTESETAD
     VDVRLRRQIL TLWQTALIRL SRLRIQDEIE VGLRYYDAAL FEVVPKINAE LRSALRSRWP
     DADLGREPIL RPGSWIGGDR DGNPYVTDEV VRQATTRAAA TALEHHLGQL ETLERELSMS
     ARLVAVTPAL DLLAAASQDD SPFRADEPYR RAVRGIRGRL TATAHRILGE APDHGLDLGL
     APYDSPRQML DELDVVDDSL RRGGDGTIAD DGLATLRDSV EVFGFHLSGL DMRQNSDVHE
     TVVAELLAWA GVHADYPSLS EDERVELLSA ELSTRRPLTT ANAEFSELTA KELAILQAGA
     DAVRTLGAGA VPNYIISMCT SVSDMLEAAV LLKEVGILDP GSGEAPSCPV GIVPLFETIE
     DLQQGAATLE ATLEVPIYRA LVSARGDAQE VMLGYSDSNK DGGYLAANWA LYRAELDLVD
     AARKTGIRLR LFHGRGGTVG RGGGPSYEAI LAQPPGAVAG SLRITEQGEV IAAKYAEPRL
     AQRNLETLLA ATLEATLLDV EGLGDDAEPA YRILDELAAL ARRAYGELVH ETPGFVEYFE
     MSTPVAEIGA LNIGSRPASR KQTTSIADLR AIPWVLSWSQ SRVMLPGWYG TGAAFEEWTQ
     GDPERVATLS RLYETWPFFR TVLSNLAMVM SKSDMGLAAR YAELVPDEEL RRRVFGKIAE
     EHERTIRMYK AVTGNDTLFA DNPGLERSVH NRFPYLEPLN HLQVELLRRY RAGDDSDQTR
     RGIQLTMNGL ATALRNSG
//
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