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Database: UniProt/TrEMBL
Entry: S5AQA2_9ALTE
LinkDB: S5AQA2_9ALTE
Original site: S5AQA2_9ALTE 
ID   S5AQA2_9ALTE            Unreviewed;       873 AA.
AC   S5AQA2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-SEP-2017, entry version 34.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
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:SAAS00635171};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=I633_17875 {ECO:0000313|EMBL:AGP79223.1};
OS   Alteromonas mediterranea 615.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas.
OX   NCBI_TaxID=1300253 {ECO:0000313|EMBL:AGP79223.1, ECO:0000313|Proteomes:UP000014909};
RN   [1] {ECO:0000313|EMBL:AGP79223.1, ECO:0000313|Proteomes:UP000014909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN='English Channel 615' {ECO:0000313|Proteomes:UP000014909};
RX   PubMed=23729633; DOI=10.1093/gbe/evt089;
RA   Lopez-Perez M., Gonzaga A., Rodriguez-Valera F.;
RT   "Genomic Diversity of "Deep Ecotype" Alteromonas macleodii Isolates:
RT   Evidence for Pan-Mediterranean Clonal Frames.";
RL   Genome Biol. Evol. 5:1220-1232(2013).
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:SAAS00730191}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00635164};
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:SAAS00635168}.
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DR   EMBL; CP004846; AGP79223.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGP79223; AGP79223; I633_17875.
DR   KEGG; amh:I633_17875; -.
DR   PATRIC; fig|1300253.3.peg.3742; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000014909; 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   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:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000014909};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AGP79223.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157}.
FT   ACT_SITE    133    133       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    538    538       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   873 AA;  98248 MW;  A1777EC687856940 CRC64;
     MQTHYDAELK DTVRYLGKTL GETIKNQLGQ EWLDRIEKIR KGGRASYQGD ATCSEELKET
     FKTMSDSDLL TVGRAFAQFL NLGNIAEQEY NAAMNVDASI DALFKHLDKA ELTADKVQDA
     VAKLNIDLVL TAHPTEVTRR TLIHKHKELA DCLQAVHQAS LSDVERKKIE TRIADLIAQA
     WHTEEIRSVR PTPVDEARWG FSVIENSLWE AVPDFMRELD GRLNEDYDVS LPLDASPVQF
     SSWMGGDRDG NPFVTSKVTE QVLLLARKRA AKLFALDLDR LQVELSMYDC NEELRDKVGD
     ANEPYRALLR PLVNKFIATR DGIADYLAGK NPDTSNWIES DDELIEPLML CYQSLIDCGM
     QVVANGLLLD TIRRARVFGI HLLRLDVRQD SERHADVFSE LTRYLGLGDY AQWSEADKQA
     FLLRELGSKR PLFPAQWDAS DDVKEVLDTC KVIAKHSKHG FGIYIISMAS EPSDVMAVQL
     LLQESGVDWP MPVAPLFETL DDLNNSPDVM RKLLSIDWYR GYVKGRQFVM IGYSDSAKDA
     GALAAGWAQY QSQEALVAIA EEFDVSLTLF HGRGGTIGRG GLPAHAAIYS QPPGSLEGGF
     RVTEQGETIR YKFGMPKLAK RSLGIYASAI IEAMLFPPPA PKEEWRELIT TMAAQGRDNY
     RATVRHDEEF VPYFRVATPE QELGKLPLGS RPAKRKPQGG IESLRAIPWI FAWAQTRLVL
     PSWLGVMRAI DSVKTPENEK VVNEMFSEWP FYRSRLSMLD MVFHKADPRI SEAYDERLVP
     KELKHFGEAL RSELKESISS LLAITGDDDI MKNDPQGKES MEIRAGYLQP LHYLQIELLD
     RIRKAGDDAQ NTSLERAMMV TIAGIAIGMR NTG
//
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