ID   CAPP_PECCP              Reviewed;         879 AA.
AC   C6DI86;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
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=PC1_4065;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT15080.1; -; Genomic_DNA.
DR   RefSeq; WP_015842157.1; NC_012917.1.
DR   AlphaFoldDB; C6DI86; -.
DR   SMR; C6DI86; -.
DR   STRING; 561230.PC1_4065; -.
DR   KEGG; pct:PC1_4065; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002736; 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.
FT   CHAIN           1..879
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000212178"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        546
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   879 AA;  98620 MW;  5C70F63A512DC688 CRC64;
     MNEQYSAMRS NVSMLGKLLG DTIKEALGEN ILDKVETIRK LSKSSRAGNE KHRQELLTTL
     QNLSNDELLP VARAFSQFLN LTNTAEQYHT ISPHGEAASN PAQLSSAFER LKESKDLTER
     DIRDAVESLS IELVLTAHPT EITRRTLIHK LVEVNTCLKQ LDHNDLADYE RNQIMRRLRQ
     LIAQSWHTDE IRKIRPTPVD EAKWGFAVVE NSLWEGVPAF LRELDEQLEQ AFGYRLPVDA
     VPVRFTSWMG GDRDGNPNVT AEVTRHVLLL SRWKAADLFL RDIQVLVSEL SMSECTPELL
     ELAGGSEVQE PYRAIMKSLR SQLSSTLSYL EARLTGEERL PPKDLLITNE QLWEPLHACY
     QSLKSCGMGI IADGRLLDTL RRVRCFGVPL VRIDVRQEST RHTEALAEIT RYLGLGDYES
     WSESDKQAFL IRELSSKRPL LPRYWEPSAD TKEVLDTCRV IAKAPQGSIA AYVISMARTP
     SDVLAVHLLL KEAGCSFALP VAPLFETLDD LNNADDVMTQ LLSIDWYRGF IQGKQMVMIG
     YSDSAKDAGV MAASWAQYRA QDALIKTCEK AGIALTLFHG RGGSIGRGGA PAHAALLSQP
     PGSLKGGLRV TEQGEMIRFK YGLPEVTISS LALYTGAILE ANLLPPPEPK QEWHEVMDEL
     SRVSCDMYRG YVRENPDFVP YFRAATPELE LGKLPLGSRP AKRRPNGGVE SLRAIPWIFA
     WTQNRLMLPA WLGAGAALQK VVDDGKQEQL EEMCRDWPFF STRIGMLEMV FAKADLWLAE
     YYDQRLVDEK LWPLGKQLRD QLAADINIVL AISNDDHLMA DLPWIAESIA LRNVYTDPLN
     VLQAELLHRS RQQEKPDADL ELALMVTIAG VAAGMRNTG
//