ID   CAPP_NEIG1              Reviewed;         900 AA.
AC   Q5F5A9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   24-JAN-2024, entry version 95.
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=NGO2020;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) 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; AE004969; AAW90628.1; -; Genomic_DNA.
DR   RefSeq; WP_010355840.1; NC_002946.2.
DR   RefSeq; YP_209040.2; NC_002946.2.
DR   AlphaFoldDB; Q5F5A9; -.
DR   SMR; Q5F5A9; -.
DR   STRING; 242231.NGO_2020; -.
DR   KEGG; ngo:NGO_2020; -.
DR   PATRIC; fig|242231.10.peg.2435; -.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   Proteomes; UP000000535; 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..900
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166602"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        568
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   900 AA;  101122 MW;  CB3E85C494759D66 CRC64;
     MQLHILNNPK DAALAADAEF LKQSLFNLLH EEASPLVVET VKLLSTSDDS AALIEKVLPQ
     LDERQTYDLT LACGLFAQIL NIAEDVHHER RRQIHEDAGH NAAEGSLTET VRRLKAGKAD
     GKSVQRQLDN TSVTAVLTAH PTEVQRQTVL NFNRRIRALL PQRERCTNAD ALARLRREID
     TVLLGLWQTS ETRRHKLSVN DEINNGVSIF PMSFFEALPK LYRKMEHDFQ TAYPDVRVPN
     ILKIGGWIGG DRDGNPFVSG ETLRFAFRRH ADAVFRFYRS ELDKLYRELP LSIRRVKVND
     DVMALAALSP DEEIARTEEP YRRAIAYIMA RAMGKARSLG LGMGCKFGFL EPYASAQKFL
     DDLKKLQRSL IDNGSRLLAE GRLADLIRSV SVFGFHMMPL DLRQHAGKHA DVVAELFQHA
     GLEDYNSLNE EQKQAALLRE LGHQRPLYSP FITYSDHTRR ELAIFNEARK IKDEFGEDAV
     TQSIISNCEQ PGDLLALALL LKESGLLAVE NGKPHSRINI VPLFETIEAL ENACPVMETM
     FRLDWYDALL ESRGNIQEIM LGYSDSNKDG GYVTSSWCLH QAELGLVELF KKYDVRMRLF
     HGRGGSVGRG GGPSYQAILA QPAGSVAGQI RITEQGEVIT AKYADPGNAQ RNLETLVAAT
     LEASILPDKK DPDAKLMQAL SDVSFKYYRE LITHPDFIDY FLQTSPIQEI ATLNLGSRPA
     SRKTLARIQD LRAIPWVFSW MQNRLMLPAW YGFGSAVETL CEGSPETLAA LRGHAQNNPF
     FQAMLSNMEQ VMAKTDITLA ENYAGLSESP EKAKVIFGMI KEEYRRSRKA LLDLLQTEEL
     LRDNRSLARS LALRIPYLNA LNGLQVAMLK RLRKEPDNPH ALLMVHLTIN GVAQGLRNTG
//