ID S5AQA2_9ALTE Unreviewed; 873 AA.
AC S5AQA2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 03-MAY-2023, entry version 53.
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 ORFNames=I633_17875 {ECO:0000313|EMBL:AGP79223.1};
OS Alteromonas mediterranea 615.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; 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 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; CP004846; AGP79223.1; -; Genomic_DNA.
DR AlphaFoldDB; S5AQA2; -.
DR KEGG; amh:I633_17875; -.
DR PATRIC; fig|1300253.3.peg.3742; -.
DR HOGENOM; CLU_006557_2_0_6; -.
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 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:AGP79223.1}.
FT ACT_SITE 133
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 538
FT /evidence="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
//
