ID   K0CDC1_ALCDB            Unreviewed;       887 AA.
AC   K0CDC1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
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:AFT71604.1};
GN   OrderedLocusNames=B5T_03337 {ECO:0000313|EMBL:AFT71604.1};
OS   Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS   B-5) (Alloalcanivorax dieselolei).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alloalcanivorax.
OX   NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT71604.1, ECO:0000313|Proteomes:UP000006286};
RN   [1] {ECO:0000313|EMBL:AFT71604.1, ECO:0000313|Proteomes:UP000006286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC   {ECO:0000313|Proteomes:UP000006286};
RX   PubMed=23144414; DOI=10.1128/JB.01813-12;
RA   Lai Q., Li W., Shao Z.;
RT   "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL   J. Bacteriol. 194:6674-6674(2012).
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, ECO:0000256|HAMAP-
CC         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; CP003466; AFT71604.1; -; Genomic_DNA.
DR   RefSeq; WP_014995666.1; NC_018691.1.
DR   AlphaFoldDB; K0CDC1; -.
DR   STRING; 930169.B5T_03337; -.
DR   KEGG; adi:B5T_03337; -.
DR   PATRIC; fig|930169.3.peg.3295; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000006286; 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:AFT71604.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006286}.
FT   ACT_SITE        144
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        553
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   887 AA;  100379 MW;  9F4D5E3E31ACE5DC CRC64;
     MEQDQHAPLR EDVRWLGELL GHTLREQVGE NLYETVERIR LAAVETRSND EMSVARLRAL
     LDPLEDDALL EVARAFSQFL NLANIAEQHH RERLHRQHQR YPGDPDSDQG LRNVLERLSA
     RQVSAQTVRD TLTDLSVELV LTAHPTEVTR RTLIRKYDQM ADLLTESDRP DLTGEERQRL
     EQRLRELIIS AWSTDEIRRE RPTPVDEAKW GFATIEQSLW RAVPDFMRQL DEELQQAGLP
     SPPADWVPVR LASWMGGDRD GNPNVTAAVT REVLLLARWM AADLYLRDVE NLLADLSMHR
     ASDELLARTG PSHEPYRVVL RDVRDRLKVT RRRMEALVEE RPVPDGEGFL NGAQLRDELR
     LLDRSLRAVG LESIANGQLK DTLRRLSCFG ITLLCLDVRQ ESGRHADTVD AITRYLELGS
     YLEWDEAERQ RFLLTELENR RPLVDDLFYQ SELCDPQVRE VLDTCKVIAE QGPEGLGAYV
     ISMAHAPSDV LAVMLLQKIA GVTRPMRVVP LFETLDDLDN AGETMSALLS IPFYRERVKG
     GQEVMIGYSD SAKDAGFLGA AWAQFRAQEK LTALFREHGI PLTLFHGRGG SISRGGSPTR
     MALLSQPSGS VAGRIRVTEQ GEVIRFKYGR PSVAAFNLEQ YVAATLEATL LPPREPQPQW
     REQMEKLTRV SVEGYRQVVR DDPALVRYLR TVTPETELSR LALGSRPARR KSDGGIESLR
     AIPWVFAWTQ IRLMLPAWLG TGAALEAALQ DQSDTDQVRE MASHWPFFQG VVDMLEMVLA
     KADSRVAAWY EERLTDDADL MRLGDSLRQR LAGTVEALGR LTGRGDLLDN NPVMRWSIRV
     RDPYTDPLHL LQAELMARLR DRDSDRVLES ALMVTIAGIA AGLRNTG
//