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   03-MAR-2009, entry version 21.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPCase;
DE            Short=PEPC;
DE            EC=4.1.1.31;
GN   Name=ppc; OrderedLocusNames=ABO_0680;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + CO(2).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
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DR   EMBL; AM286690; CAL16128.1; -; Genomic_DNA.
DR   RefSeq; YP_692400.1; -.
DR   GeneID; 4212270; -.
DR   GenomeReviews; AM286690_GR; ABO_0680.
DR   KEGG; abo:ABO_0680; -.
DR   NMPDR; fig|393595.12.peg.680; -.
DR   HOGENOM; Q0VRS0; -.
DR   BioCyc; ABOR393595:ABO_0680-MON; -.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:HAMAP.
DR   GO; GO:0015977; P:carbon utilization by fixation of carbon di...; IEA:HAMAP.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP.
DR   HAMAP; MF_00595; -; 1.
DR   InterPro; IPR001449; PEP_COase.
DR   InterPro; IPR018129; PEP_COase_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase_cat.
DR   Gene3D; G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation; Complete proteome; Lyase;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    888       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_1000025546.
FT   ACT_SITE    144    144       By similarity.
FT   ACT_SITE    553    553       By similarity.
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
//