ID   CAPP_ACIAD              Reviewed;         894 AA.
AC   Q6F6Q6;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=ACIAD3627;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG70261.1; -; Genomic_DNA.
DR   RefSeq; WP_011182842.1; NC_005966.1.
DR   AlphaFoldDB; Q6F6Q6; -.
DR   SMR; Q6F6Q6; -.
DR   STRING; 62977.ACIAD3627; -.
DR   EnsemblBacteria; CAG70261; CAG70261; ACIAD3627.
DR   GeneID; 45235790; -.
DR   KEGG; aci:ACIAD3627; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
DR   BioCyc; ASP62977:ACIAD_RS16400-MON; -.
DR   Proteomes; UP000000430; 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..894
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166577"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        556
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   894 AA;  102249 MW;  D91DBD3AB0101C9C CRC64;
     MIQQIDAPLR EDVRLLGNLL GETLKQHAGQ DLFNQIEQIR ALAKGARDGQ AETEKKLEQL
     FLDLKDEEIL PLTRAFSYFL NFANIAEQYH VVRSRRRSEF DEQGPPPNPL IHLFEKFKQN
     QISSKQLFQQ VSNLSIELVL TAHPTEVSRR TLIQKYDDIN EGLSKLDQQK LTPRERQQVL
     DDLKQLICSA WQTDEIRQNK PTPLDEAKWG FTTIEQTLWN AVPKFVRELD TLVHQHCDAH
     LPLDISPIRF ASWMGGDRDG NPNVTHNVTQ EVLWLSRWQA ADLYLRDIED LRWELSIQAC
     SEELSQTLGR RHPEPYREYL RSTRERLKAT RQWLSLRLQG LDGDDSQIIR HKQELLDPLL
     LCHRSLMECN LPEIANGKLL DFIYRVNCFG IELLKLDIRQ ESGRHRQAIS AITEYLGLGN
     FESWTEQARQ NFLIQELQSK RPLLPKYLNE PEGSLIEHPD VKEVFATMRT LAEQPPESLG
     AYIISMAEYA SDVLAVLLLQ KEAGILQPLR VVPLFETLKD LDGAAKTMET LFNMHWYKQH
     IQGKHEVMIG YSDSAKDAGF MSANWAQYRA QEELTAVAKS HGVQLTLFHG RGGSISRGGA
     PTQQALFSQP PGSISGAIRV TEQGEMIRFK FGLEGVALQN LEIYTAATLE ATLLPPPVPK
     QEWRDLMHQM TDISVRVYRE TVRENPHFVQ YLRTVTPELE LQMLPLGSRP AKRKVSGGIE
     SLRAIPWVFA WTQIRLMLPA WLGTGAAINQ VIDENKKAVL DEMLAEWPYF QTLIDMLEMV
     LSKSDANIAL YYESHLTDNE DLKILGEMLR QRLNDAVQTL LSMKGESKLL SKNDVLDQAM
     QVRKPYLLPL HLLQAELMKR RRLYTAQSNA ERTPVDHALM VSIAGIAAGL RNTG