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CAPP_HISS2
ID   CAPP_HISS2              Reviewed;         879 AA.
AC   B0UUJ3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=HSM_1472;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) 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;
CC         Evidence={ECO:0000255|HAMAP-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; CP000947; ACA31221.1; -; Genomic_DNA.
DR   RefSeq; WP_012340613.1; NC_010519.1.
DR   AlphaFoldDB; B0UUJ3; -.
DR   SMR; B0UUJ3; -.
DR   STRING; 228400.HSM_1472; -.
DR   EnsemblBacteria; ACA31221; ACA31221; HSM_1472.
DR   KEGG; hsm:HSM_1472; -.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; GPTHRFI; -.
DR   OrthoDB; 398146at2; -.
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   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.
FT   CHAIN           1..879
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000082427"
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;  99884 MW;  5D6A8CD1A0653EC4 CRC64;
     MPQKYSTLKN NINMLGHFLG ETISDAQGSD ILDLIENIRV LSRDSRSGDE KAREKLLDTL
     STISNENIIP VARAFSQFLN LTNIAEQYQT ISRKHIDQVA SDRSLEALFE RLKAQNVPAE
     KVISTVEKLL IELVLTAHPT EVTRRSLLHK YVEINRCLSR LEHDDLTQSE STKLKRRLMQ
     LIALAWHTNE IRTQRPTPVD EAKWGIAVIE NSLWKAVPDF CRQLNLHLEK NFGVQHSVNL
     APVKFSSWIG GDRDGNPFVT AETTRQVLIM NRWKAAELFL ADIQVLSEEL SVVHCTEEFR
     AKYGDHLEPY RVVVKNLRAK LVKTVAYYGE ILENKPSTIN TNDILTDDQQ LWEPLYDCYQ
     SLHQCGMRII ANGILLDCLR RIRCFGLSLS HLDIRQESLR HTKALSEITR YIGLGDYSQW
     MEDDKQAFLI RELSSRRPLL PRNWTPSPET QEILETCRVI AQQPEGVISC YIISMARTAS
     DVLAVHLLLK EAGVTYYLPV VPLFETLDDL NASKEVMTQL FNVGWYRGVI NNKQMVMIGY
     SDSAKDAGMM AASWAQYRAQ EQLVNLCEKM GVELTLFHGR GGTIGRGGAP AHAALLSQPP
     RSLKNGLRVT EQGEMIRFKL GLPAVAVNSF DLYASAILEA NLLPPPEPKE SWRAIMNELS
     DSSCNIYRSV VRGDKDFVPY FRSATPEQEL SKLPLGSRPS KRNPNGGVES LRAIPWIFAW
     MQNRLMLPAW LGASASIRQS IEKGNKETIE EMCKNWPFFS TRIGMLEMVF SKTDTWLSEH
     YDLNLVKKEL WYLGQSLREQ LQADIKTILS LSHEDELMSD LPWIAESIAL RNIYTDPLNL
     LQVELLRRLR ENPENPNPDV EQALMITITG IAAGMRNTG
 
 
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