ID   CAPP_AERHH              Reviewed;         877 AA.
AC   A0KFU8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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}; OrderedLocusNames=AHA_0591;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC   2358 / NCIMB 9240 / NCTC 8049;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(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;
CC         Evidence={ECO:0000255|HAMAP-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; CP000462; ABK39687.1; -; Genomic_DNA.
DR   RefSeq; WP_005308531.1; NC_008570.1.
DR   RefSeq; YP_855124.1; NC_008570.1.
DR   AlphaFoldDB; A0KFU8; -.
DR   SMR; A0KFU8; -.
DR   STRING; 380703.AHA_0591; -.
DR   EnsemblBacteria; ABK39687; ABK39687; AHA_0591.
DR   GeneID; 58197610; -.
DR   KEGG; aha:AHA_0591; -.
DR   PATRIC; fig|380703.7.peg.587; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   PRO; PR:A0KFU8; -.
DR   Proteomes; UP000000756; 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   PANTHER; PTHR30523; PTHR30523; 1.
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; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..877
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025544"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        543
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   877 AA;  99020 MW;  6EF0B3ECC2774D19 CRC64;
     MNEKYAALRA NVGMLGQLLG KSIKDHQGQA FLDKIETIRQ LAKSSRKGNE TDRERLLDTL
     RNLSDDELLP VARAFSQFLN LANVAEQFHT ISRRCEEQVC TPDPLEQMFD KLKASNLSQE
     AIIQAVRELD IDLVLTAHPT EVTRRTLIHK HVQLNDCLEA LELSDLLPRE RDKILNRIEQ
     LVNQAWHTNE IREQRPTPVD EAKWGFAVVE NSLWPAIPEF MRNLDERLQH HLGVRLPLDA
     APVKFTSWMG GDRDGNPFVT AKVTAEVLEL GRWMAVSLFY KDIKELTSEL SMSDCTDAVR
     ERVGDHPEPY RALVRELREQ LRETQEFLTA KVQGQASESR DLVKTTAQLR EPLELCYHSL
     HACGMGNIAD GMLLDVLRKL ACFGIHLVKL DIRQDGERHG QVFSELTRYL GMGDYAEWSE
     DDKQAFLLNE LNSRRPLIPT DWEPSDETRE TLDTCKVIAQ HDPDAFGIYI ISMAGAPSDV
     LAVQLLLKEA GCKFRMPVAP LFETQEDLMA GTAVMERLLS VDWYRGYIQG RQYVMIGYSD
     SAKDAGMMAA GWAQYAAMES LVALAEANNL RLTLFHGRGG TVGRGGAPAH QAILSQPPGS
     LRGGLRVTEQ GEMIRFKFGL PKVAIQSLNL YTSAVLEGNL LPPPKPKECW RAVMEQLASV
     SCDHYRSIVR GHPDFVPYFR AATPEMELGK LPLGSRPSKR KPNGGVESLR AIPWIFAWTQ
     NRLMLPAWLG AHKGLQQAIA DGQKGVLEEM SRQWPFFRTR LEMLEMVFLK ADVWLAEYYD
     TRLVPKELWG LGKQLRQELA DSIQVVLELR PQGDLLDDQP WIKESIKLRN PYTDPLNVLQ
     VELLGRSRNH AETLHPELDQ ALMVTIAGIA AGMRNTG