ID   CAPP_NEIMF              Reviewed;         900 AA.
AC   A1KWE0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
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=NMC2042;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM421808; CAM11197.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1KWE0; -.
DR   SMR; A1KWE0; -.
DR   KEGG; nmc:NMC2042; -.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   Proteomes; UP000002286; 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..900
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025568"
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;  101160 MW;  67602FA07423EF9C CRC64;
     MQLHILNNPK DAALAADAEF LKQSLFNLLH EEASPLVVET VKLLSTSDDS AALIEKVLPQ
     LDEQQTHDLT LACGLFAQIL NIAEDVHHER RRQIHEEAGR GGAEGSLTET VRRLKAGKAD
     GKSVQRQLDN TSVTAVLTAH PTEVQRQTVL SFNRRIRALL PQRERCTNAD ALARLRREID
     TILLGLWQTS ETRRHKLSVN DEINNGVSIF PMSFFEALPK LYRNMEHDFQ MVYPDVCVPN
     ILKIGGWIGG DRDGNPFVSA ETLRFAFRRH ADAVFRFYRG ELDKLYRELP LSIRRVKVND
     DVMALAALSP DEELARTEEP YRRAIAYIMA RAMGKARALG LGMGCKFGFL EPYASAQEFL
     DDLKKLQRSL IDNGSRLLAE GRLADLIRSV SVFGFHMMPL DLRQHAGKHA DVVAELFQHA
     GLEDYNSLNE EQKQAVLLRE LSHQRPLYSP FITYSDHTRH ELAIFNEARK IKDEFGEDAV
     TQSIISNCEQ PSDLLALALL LKESGLLAVE NGKPHSRINI VPLFETIEAL ENACPVMETM
     FRLDWYDALL ESRGNIQEIM LGYSDSNKDG GYVTSSWCLY QAELGLVELF KKYDVRMRLF
     HGRGGSVGRG GGPSYQAILA QPAGSVAGQI RITEQGEVIT AKYADPGNAQ RNLETLVAAT
     LEASILPDKK DPDAKLMQAL SDVSFKYYRE LITHPDFIDY FLQTSPIQEI ATLNLGSRPA
     SRKTLARIQD LRAIPWVFSW MQNRLMLPAW YGFGSAVETL CEGNPDTLTA LREHAQSNPF
     FQAMLSNMEQ VMAKTDITLA ENYAGLSESP DKAKIIFGMI KEEYRRSRKA LLDLLQTEEL
     LRDNRSLARS LALRIPYLNA LNGLQVAMLK RLRKEPDNPH ALLMVHLTIN GVAQGLRNTG
//