ID   CAPP_NEIMB              Reviewed;         900 AA.
AC   Q9JXG5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-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=NMB2061;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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}.
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; AE002098; AAF42380.1; -; Genomic_DNA.
DR   PIR; A81010; A81010.
DR   RefSeq; NP_275051.1; NC_003112.2.
DR   RefSeq; WP_002244350.1; NC_003112.2.
DR   AlphaFoldDB; Q9JXG5; -.
DR   SMR; Q9JXG5; -.
DR   STRING; 122586.NMB2061; -.
DR   PaxDb; Q9JXG5; -.
DR   EnsemblBacteria; AAF42380; AAF42380; NMB2061.
DR   KEGG; nme:NMB2061; -.
DR   PATRIC; fig|122586.8.peg.2639; -.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
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..900
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166604"
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;  101210 MW;  489B26F74AA06012 CRC64;
     MQLHILNNPK DAALAADAEF LKQSLFNLLH EEASPLVVET VKLLSTSDDS AALIEKVLPQ
     LDEQQTHDLT LACGLFAQIL NIAEDVHHER RRQIHEEAGR GGAEGSLTET VRRLKAGKAD
     GKSVQRQLDN TSVTAVLTAH PTEVQRQTVL SFNRRIRALL PQRERCTNAD ALARLRREID
     TILLGLWQTS ETRRHKLSVN DEINNGVSIF PMSFFEALPK LYRKMEHDFQ TAYPGVRVPD
     ILKIGGWIGG DRDGNPFVSA ETLRFAFRRH ADAVFRFYRG ELDKLYRELP LSIRRVKVNG
     DVTALSDKSP DEEIARAEEP YRRAIAYIMA RAMGKARALG LGMGCKFGFL EPYASAQEFL
     DDLKKLQRSL IDNGSRLLAE GRLADLIRSV SVFGFHMMPL DLRQHAGKHA DVVAELFQHA
     GLEDYNRLNE EQKQTALLRE LSHQRPLYSP FITYSDHTRH ELAIFNEARK IKDEFGEDAV
     TQSIISNCEQ PSDLLALALL LKETGLLAVE 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 CEDKPETLAA LREHAQSNPF
     FQAMLSNMEQ VMAKTDITLA ENYAGLSESP DKAKIIFGMI KEEYRRSRKA LLDLLQTEEL
     LRDNRSLARS LALRIPYLNA LNGLQVAMLK RLRKEPDNPH ALLMVHLTIN GVAQGLRNTG