ID   CAPP_ALCBS              Reviewed;         888 AA.
AC   Q0VRS0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=ABO_0680;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
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DR   EMBL; AM286690; CAL16128.1; -; Genomic_DNA.
DR   RefSeq; WP_011587965.1; NC_008260.1.
DR   AlphaFoldDB; Q0VRS0; -.
DR   SMR; Q0VRS0; -.
DR   STRING; 393595.ABO_0680; -.
DR   KEGG; abo:ABO_0680; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000008871; 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; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..888
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025546"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        553
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   888 AA;  99098 MW;  2CC2ADF5B3B8B74F CRC64;
     MDHNVNAPLR DDVRLLGDLL GECLRQQAGD SIYETVEKIR QASVATRTEG GASLASLRDL
     LSPLDDATLL EVARAFSQFL NLSNIAEQHH RERLHRQHQR YPGDAGTDQG LQEVLQRLAD
     NDIAKEQISG TLEQLSVELV LTAHPTEVTR RTLIRKYDQM ADLLSELDRP DFNEDERELR
     RERLRRVILA AWCTDEIRRE KPTPVDEAKW GFATIEQSLW QAVPDVLRQL EAQLADRGLP
     APPSDWAPVK LASWMGGDRD GNPNVTAPVT REVLLLARWM AADLYLRDVE NLLADLSMKS
     ASEELLAATG PTHEPYRVLL REVRSRLRLT RRQMEAQVEG LPVPEGQAYL RREELMAPLQ
     LLDRSLRAVG LSDIADGDLK NTLRRLNCFG ITLLRLDIRQ ESTRHSDVLD AITRYLQLGR
     YSDWDEAARQ AFLVDELQAR RPLIDAAFRD SEHCTAEVAE VLATCEVIAE QGSEGLGAYV
     ISMATTPSDV MAVMLLQKIA GVREPMRVVP LFETLDDLDG AEQTMSALLA LPFYRERVAA
     GQEIMIGYSD SAKDAGFLGA AWAQYRAQEK LTALFADNGI PLTLFHGRGG SISRGGSPTR
     MALLSQPPGS VAGRIRVTEQ GEVIRFKYGR PSVAVFNLEQ YVAATLEATL LPPQAARPEW
     RQQMQALTDT SVAGYRGVVR DEPELVRYLR TVTPETELSR LALGSRPARR KSDQGISSLR
     AIPWVFAWTQ IRLMLPAWLG TGAALEDAQN DAAQHAMVRE MASEWPFFQG VVDMLEMVLA
     KSDLRVAAWY EERLAGDDPG LMRLGEVLRE RLTATVSALS ALTGREDLLD NNPVMRWSIR
     VRDPYTDPLH LLQAELMARL RQQDGDETLE SALMVTIAGI AAGLRNTG
//