ID   CAPP_HAEIN              Reviewed;         879 AA.
AC   P43920;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPC;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
GN   Name=ppc; OrderedLocusNames=HI_1636;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; L42023; AAC23281.1; -; Genomic_DNA.
DR   PIR; I64133; I64133.
DR   RefSeq; NP_439778.1; NC_000907.1.
DR   AlphaFoldDB; P43920; -.
DR   SMR; P43920; -.
DR   STRING; 71421.HI_1636; -.
DR   EnsemblBacteria; AAC23281; AAC23281; HI_1636.
DR   KEGG; hin:HI_1636; -.
DR   PATRIC; fig|71421.8.peg.1712; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   PhylomeDB; P43920; -.
DR   BioCyc; HINF71421:G1GJ1-1653-MONOMER; -.
DR   Proteomes; UP000000579; 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   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..879
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166597"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        545
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   879 AA;  100055 MW;  3E45E42C2D62DF40 CRC64;
     MTQEYSTLRN NISMLGRFLG ETINDAQGED ILELIENIRK LSRNSRAGDD KARQALLDTL
     GSISNENIIP VARAFSQFLN LTNIAEQYQT ISREHSLAQS SSQSLSELFK RLKEQNASVE
     EVHKTVEKLL IELVLTAHPT ETTRRSLIHK HIEINKCLSK LEHHDLTEKE RNIIERLLLR
     LIAEAWHTNE IRTVRPTPFD EAKWGFAMLE NSLWQAVPEF LRQLNETARE FLGYDLSVGL
     KPVRISSWMG GDRDGNPFVT AQITKKVLYF ARWKAADLFL QDISKLADEL SMMKCSDEFR
     DKYGEHLEPY RFVVKNLRNQ LTATLAYFDD HLSNRTPRVS ESEIILEDNQ LWEPLYDCYQ
     SLIQCGMRII ANGSLLNILH 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 LGAGAAIRQV IEQGKGDIIH KMCENWPFFS TRIGMLEMVF SKSDTWLSQQ
     YDQRLVKKEL WYLGENLRKQ LEDDIQTVLS LSHQSELMSD LPWIADSIAL RNIYTDPLNL
     LQVELLHRFR ENPEQVNPDV EQALMITITG IAAGMRNTG
//