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KATG_COLP3
ID   KATG_COLP3              Reviewed;         740 AA.
AC   Q486C8;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE            Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE            EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE   AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
DE   Flags: Precursor;
GN   Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=CPS_1344;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC       {ECO:0000255|HAMAP-Rule:MF_01961};
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC   -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC       for the catalase, but not the peroxidase activity of the enzyme.
CC       {ECO:0000255|HAMAP-Rule:MF_01961}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR   EMBL; CP000083; AAZ28741.1; -; Genomic_DNA.
DR   RefSeq; WP_011042181.1; NC_003910.7.
DR   AlphaFoldDB; Q486C8; -.
DR   SMR; Q486C8; -.
DR   STRING; 167879.CPS_1344; -.
DR   PeroxiBase; 2698; CpsCP01.
DR   EnsemblBacteria; AAZ28741; AAZ28741; CPS_1344.
DR   KEGG; cps:CPS_1344; -.
DR   eggNOG; COG0376; Bacteria.
DR   HOGENOM; CLU_025424_2_0_6; -.
DR   OMA; EEIFWGP; -.
DR   OrthoDB; 49441at2; -.
DR   Proteomes; UP000000547; Chromosome.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   HAMAP; MF_01961; Catal_peroxid; 1.
DR   InterPro; IPR000763; Catalase_peroxidase.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   PANTHER; PTHR30555; PTHR30555; 1.
DR   Pfam; PF00141; peroxidase; 2.
DR   PRINTS; PR00460; BPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 2.
DR   TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 2.
PE   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CHAIN           28..740
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354765"
FT   ACT_SITE        107
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         269
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   SITE            103
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        106..228
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   254)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        228..254
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   106)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   740 AA;  81126 MW;  43448DB0C34083B3 CRC64;
     MFKSTLPIAA AISVALTSMV LPAKALAANE AKTNQFWWPD QLSLSPLRQH GAESNPYGEQ
     FNYAKEFASL DLAMLKKDIQ TTLTDSKSWW PADWGHYGPL MIRMAWHSAG VYRVHDGRGG
     ASGGQQRFAP LNSWPDNVNL DKARRLLWPV KQKYGRKISW ADLMVLSGNV ALESMGFKTF
     GFAGGRTDDW EPDLVYWGPE TAMLSDKRRD KKGKLKGPLA AVEMGLIYVN PEGPHGKPDP
     LLAANDIRMS FGRMAMNDEE IVALLAGGHT LGKAHGAKKP NGCVGAEPAA ADIEAQGLGW
     KNKCGTGVGA DTISSGLEGA WTVTPTQWSS NYLDNLMNFN WVLTKSPAGA KQWIPDNKAA
     ANLVPDAHIP NKRHAPIMFT TDIALKEDPQ FRKIVERFRA DPTQFDLAFA KAWFKLTHRD
     MGPRARYVGA EVPSEVLMWQ DPIPAINYQL ITDKDIKQLK KQITNSGLTT SELVRTAWAA
     ASSHRVTDMR GGANGARINL EPQNSWAVNN PKELGKVLAK LEGIQARFNK KSAKTKVSLA
     DVIVLGGATA IENAAAKAGN RITVPFSPGR ADASQAQTNV KSFNYLKPKA DGFRNFYTDD
     SYSSPAEMLV DKANSLGLNV PEMTVLIGGM RALDANYDAS SYGVLTNNPG VLTNDFFVNL
     LDMKTVWSKD KSNAGIYIGH DRASGTEKWQ ATPVDLIFGS SSELRAIAEV YASDDADKKF
     INDFTKAWVK VMQLDRFDLK
 
 
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