ID   CAPP_HAEIG              Reviewed;         879 AA.
AC   A5UIY9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
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};
GN   OrderedLocusNames=CGSHiGG_09900;
OS   Haemophilus influenzae (strain PittGG).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittGG;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(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; CP000672; ABR00745.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5UIY9; -.
DR   SMR; A5UIY9; -.
DR   KEGG; hiq:CGSHiGG_09900; -.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000001990; 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..879
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025561"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        545
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   879 AA;  100109 MW;  976B10BDF36EBE3C CRC64;
     MTQEYSTLRN NISMLGRFLG ETINDAQGED ILELIENIRK LSRNSRAGDD KARQALLDTL
     GSISNENIIP VARAFSQFLN LTNIAEQYQT ISREHSLAQS SSQSLSELFK RLKEQNASVE
     EVHKTVEKLL IELVLTAHPT ETTRRSLIHK HIEINKCLSK LEHHDLTEKE RNIIERLLLR
     LIAEAWHTNE IRTVRPTPFD EAKWGFAMLE NSLWQAVPEF LRQLNETTRE FLGYDLPVGL
     KPVRISSWMG GDRDGNPFVT AQITKKVLYF ARWKAADLFL QDISKLADEL SMMKCSDEFR
     DKYGEHLEPY RFVVKNLRNQ LTATLAYFDD HLSNRTPRVS ESEIILEDNQ LWEPLYDCYQ
     SLIQCGMRII ANGSLLDILH RISCFGVTLS QMDIRQESTR HTDAIAEITR YIGLGDYSQW
     MEDDKQAFLI RELSSRRPLI PQNWTPSPET KEILDTCKVI AQQKQGVIAC YVISMARSAS
     DVLAVHLLLK ESGVPYHIPV VPLFETLEDL DAAEKVMTQL FNVGWYRGVI NNRQMVMIGY
     SDSAKDAGMM AASWAQYRAQ EALVNLTEKL GIELTLFHGR GGTIGRGGAP AHAALLSQPP
     RSLKNGLRVT EQGEMIRFKL GLPAVAVETF DLYASAILEA NLLPPPEPKP EWRTIMDELS
     TISCDIYRGV VRGDKDFVPY FRSATPEQEL SKLPLGSRPA KRNPNGGVES LRAIPWIFAW
     MQNRLMLPAW LGAGAAIRQI IEQGKGDIIH KMCENWPFFS TRIGMLEMVF SKSDTWLSQQ
     YDQRLVKKEL WYLGENLRKQ LEDDIQTVLS LSHQSKLMSD LPWIADSIAL RNIYTDPLNL
     LQVELLHRFR ENPEQVNPDV EQALMITITG IAAGMRNTG
//