ID   CAPP_VEREI              Reviewed;         930 AA.
AC   A1WGR0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
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=Veis_1041;
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL   Submitted (DEC-2006) 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; CP000542; ABM56817.1; -; Genomic_DNA.
DR   RefSeq; WP_011808829.1; NC_008786.1.
DR   AlphaFoldDB; A1WGR0; -.
DR   SMR; A1WGR0; -.
DR   STRING; 391735.Veis_1041; -.
DR   GeneID; 76459715; -.
DR   KEGG; vei:Veis_1041; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000000374; 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; Reference proteome.
FT   CHAIN           1..930
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025600"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        586
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   930 AA;  102615 MW;  6C229CB95AE88753 CRC64;
     MQPADKDLPL MDDIRLLGRI LGDVIREQEG PRVYALVEQV RKLSVSFRRD ADQEADRALK
     KLLESLSTGQ TVGVIRAFTY FSHLANLAED RHRIRRRAVH ERAGDTQEGS IELALARLRA
     AGIAPQTIAQ TLAGSHVAPV LTAHPTEVQR KSILDAERSI AQLLAERDDI QARARLYDGA
     NDALTPRALA ANEALLRARV TQLWQTRLLR YSKLTVADEI ENALSYYEAT FLREIPEIYA
     ALENALGQHP VHSFLRMGQW IGGDRDGNPN ATAQTLQYAL GRQAEVALRH YLTEVHYLGG
     ELSLSTRLVQ VSAPMQALAL RSPDRNEHRQ DEPYRLALTG IYARLAATLK ALTGGEAARH
     AVAPQNAYAS AQEFLADLRV IEDSLTAHHG AALAAGRLHP LIRAVQVFGF HLATVDLRQS
     SDKHELVVAE LLATARVQER YADLPEAGKR ALLIRLLNDA RPLRVVGARY SAHAQGELAI
     FETARALRER FGAEAIRHYI ISHTETMSDL LEVLLLHKEV GLMSGTLDDA AARNQLIVVP
     LFETIADLRN AAPIMREFYA LPGVAALVQR SGGEQDIMLG YSDSNKDGGI FTSNWELYRA
     EIALVQLFDE LAASHGIQLR MFHGRGGTVG RGGGPSYQAI LAQPPGTVRG QIRLTEQGEV
     IASKYANPEI GRRNLEILVA ATLEATLLQP TKPAPKTFLA AAGQLSQASM AAYRALVYET
     PGFTEYFFNA TPIREIAELN IGSRPAARKA SQKIEDLRAI PWGFSWGQCR LTLPGWYGFG
     AAVAAFVNLQ GKTPGAQLAL LQRMYRQWPF FRTLLSNMDM VLAKSDLALA GRYSELVSDA
     RLRKKVFAAI EAEWHSTADA LSRITGDQQR LAHNSALARS IKHRFAYIDP LHHLQVELVR
     RWRAGQDDER VQTGIHISIN GIAAGLRNTG
//