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CAPP_HAES1
ID   CAPP_HAES1              Reviewed;         879 AA.
AC   Q0I371;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=HS_0994;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129Pt;
RX   PubMed=17172329; DOI=10.1128/jb.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT   129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT   influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(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;
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; CP000436; ABI25269.1; -; Genomic_DNA.
DR   RefSeq; WP_011609148.1; NC_008309.1.
DR   AlphaFoldDB; Q0I371; -.
DR   SMR; Q0I371; -.
DR   STRING; 205914.HS_0994; -.
DR   EnsemblBacteria; ABI25269; ABI25269; HS_0994.
DR   KEGG; hso:HS_0994; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; GPTHRFI; -.
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_1000025562"
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;  99900 MW;  9168FEAF95757797 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 PRNWTPSLET 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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