ID C1B4M0_RHOOB Unreviewed; 918 AA.
AC C1B4M0;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 100.
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:BAH55209.1};
GN OrderedLocusNames=ROP_69620 {ECO:0000313|EMBL:BAH55209.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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 erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) 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; AP011115; BAH55209.1; -; Genomic_DNA.
DR RefSeq; WP_015890634.1; NC_012522.1.
DR AlphaFoldDB; C1B4M0; -.
DR STRING; 632772.ROP_69620; -.
DR KEGG; rop:ROP_69620; -.
DR PATRIC; fig|632772.20.peg.7253; -.
DR HOGENOM; CLU_006557_2_0_11; -.
DR OMA; PWVFGWT; -.
DR OrthoDB; 9768133at2; -.
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 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:BAH55209.1}.
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; 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
//