ID   CAPP_ACIBT              Reviewed;         894 AA.
AC   A3MA94;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=A1S_3449;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS   KC755 / 5377).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT   density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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; CP000521; ABO13838.1; -; Genomic_DNA.
DR   RefSeq; WP_000250585.1; NZ_CP053098.1.
DR   AlphaFoldDB; A3MA94; -.
DR   SMR; A3MA94; -.
DR   KEGG; acb:A1S_3449; -.
DR   HOGENOM; CLU_006557_2_0_6; -.
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..894
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025542"
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;  102087 MW;  84C447D1F8F14990 CRC64;
     MVQQIDAPLR EDVRLLGNLL GETLKQHAGQ ELFNQIEQIR ALAKGARDGQ AEAEKQLEQL
     FLELPDEELL PLTRAFSHFL NFANIAEQYH VVRSRRQAEF DPDANSPNPL VHLFKKFKDK
     NISTEKLFQQ ICDLKIELVL TAHPTEVSRR TLIQKYDDIN ACLSQLDQQK LTPRERQNAL
     ANLKQQISSA WQTDEIRQHR PTPVDEAKWG FATIEQTLWN AVPKFIRELN ELVQDNCQQN
     LPLHIAPVRF ASWMGGDRDG NPNVTHQITQ EVLWLSRWQA ADLYLRDIEN LRWELSIQSC
     SEEMVQAIGS PHPEPYREYL RATRERLKAT RHWLAQRLQG LEADDSNVIK SKDELLQPLL
     LCYRSLIDSN LPEIANGQLL DFIYRVNCFG IELLKLDIRQ ESGRHRQAIS AITEYLGLGN
     FESWTEQARQ NFLIQELQSK RPLLPKYINE PEGSLIGHPD VQEVFATMRT LADQPPESLG
     AYIISMAEYP SDVLAVLLLQ KEAGIQHPLR VVPLFETLKD LDGAATTMNT LFNMHWYKQH
     IQGKHEVMIG YSDSAKDAGF MSANWAQYRA QEELTAIARK HGVQLTLFHG RGGSISRGGA
     PTQQALFSQP PGSISGAIRV TEQGEMIRFK FGLEGIAMQN LEIYTAATLE ATLLPPPEPK
     AEWRELMNRM TDHSVKVYRQ TVRENPHFVK YLRTVTPELE LQMLPLGSRP AKRKVSGGIE
     SLRAIPWVFA WTQIRLMLPA WLGTGAAINE VIADQQKATL DEMLQQWPYF QTLIDMLEMV
     LSKADANIAL YYESHLTEDE DLKVLGNQLR QRLKDAVETL LTLKDESKLL SDNEVLDQSM
     QVRKPYLLPL HLLQAELMKR RRDYLAERQA EHTPVDHALM VSIAGIAAGL RNTG
//