位置:首页 > 蛋白库 > KATG1_BURA4
KATG1_BURA4
ID   KATG1_BURA4             Reviewed;         728 AA.
AC   B1YTH4;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Catalase-peroxidase 1 {ECO:0000255|HAMAP-Rule:MF_01961};
DE            Short=CP 1 {ECO:0000255|HAMAP-Rule:MF_01961};
DE            EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE   AltName: Full=Peroxidase/catalase 1 {ECO:0000255|HAMAP-Rule:MF_01961};
GN   Name=katG1 {ECO:0000255|HAMAP-Rule:MF_01961};
GN   OrderedLocusNames=BamMC406_0642;
OS   Burkholderia ambifaria (strain MC40-6).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=398577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC40-6;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA   Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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; CP001025; ACB63139.1; -; Genomic_DNA.
DR   RefSeq; WP_012363134.1; NC_010551.1.
DR   AlphaFoldDB; B1YTH4; -.
DR   SMR; B1YTH4; -.
DR   EnsemblBacteria; ACB63139; ACB63139; BamMC406_0642.
DR   KEGG; bac:BamMC406_0642; -.
DR   HOGENOM; CLU_025424_2_0_4; -.
DR   OMA; MILAGNC; -.
DR   OrthoDB; 49441at2; -.
DR   Proteomes; UP000001680; Chromosome 1.
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   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
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; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT   CHAIN           1..728
FT                   /note="Catalase-peroxidase 1"
FT                   /id="PRO_0000354731"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         259
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            88
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        91..218
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   244)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        218..244
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   91)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   728 AA;  79221 MW;  6E914122B42278BE CRC64;
     MSTESKCPFN HTAAGGTSNK DWWPNQLNLN ILHRHSALSD PMDKDFDYAQ AFKKLDLAAV
     KRDLQALMTT SQDWWPADFG HYGGLFVRMA WHSAGTYRTA DGRGGAGGGQ QRFAPLNSWP
     DNANLDKARR LLWPIKQKYG RNISWADLLI LTGNVALESM GFKTFGYAGG RADTWEPDDV
     YWGSEKIWLE LSGGPNSRYS GDRELENPLA AVQMGLIYVN PEGPDGNPDP VAAARDIRDT
     FARMAMNDEE TVALIAGGHT FGKTHGAGPA TDVGPEPEAA GIEQQGLGWK SAYASGKGHD
     AITSGLEVTW TSTPTKWSHD FFKHLFSYEW ELTKSPAGAH QWVAKGADEV IPDAFDASKK
     HRPTMLTTDL SLRFDPAYEK ISRRFYENPA EFADAFARAW FKLTHRDMGP RARYLGPEVP
     AEELLWQDPI PVVDHPLIDD ADVAALKAKV LASGLSVAQL VSTAWASAST FRGSDKRGGA
     NGARIRLAPQ KDWEVNQPAA LAAVLETLEG VRKAFNDAQT GGKKVSLADL IVLAGAAGIE
     QAAKNAGVAV TVPFAPGRMD ASQEQTDVDA MAVLEPVADG FRNYLKSAYK TPAEALLVDK
     AQLLTLNGPE LTVLVGGLRV LGANVGDAKH GVFTDRPGTL SNDFFVNLLD MGTEWKPVSA
     ANDVFEGRDR ATGLVKWTGT RVDLIFGSHS QLRALAEVYG SADANEKFVR DFVAAWDKVM
     NLDRFDLA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024