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KATG2_BURCA
ID   KATG2_BURCA             Reviewed;         728 AA.
AC   Q1BQP0;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Catalase-peroxidase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE            Short=CP 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE            EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE   AltName: Full=Peroxidase/catalase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
GN   Name=katG2 {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Bcen_3169;
OS   Burkholderia cenocepacia (strain AU 1054).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=331271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU 1054;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K.,
RA   Tiedje J.M., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia AU 1054.";
RL   Submitted (MAY-2006) 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}.
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DR   EMBL; CP000379; ABF78065.1; -; Genomic_DNA.
DR   RefSeq; WP_011546991.1; NC_008061.1.
DR   AlphaFoldDB; Q1BQP0; -.
DR   SMR; Q1BQP0; -.
DR   PeroxiBase; 3310; BcenCP02_AU1054.
DR   EnsemblBacteria; ABF78065; ABF78065; Bcen_3169.
DR   KEGG; bcn:Bcen_3169; -.
DR   HOGENOM; CLU_025424_2_0_4; -.
DR   OMA; KWTATRM; -.
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 2"
FT                   /id="PRO_0000354733"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         255
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..214
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   240)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        214..240
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   91)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   728 AA;  79926 MW;  24FBBA5BA38AAB9C CRC64;
     MSNEGKCPFN HGKRNGTTNR DWWPNQLNLK ILHQHSSEAD PMDPGFDYAE AFNSLDLAAV
     KADLRALMTA SQDWWPADFG HYGPFFVRMA WHSAGTYRTG DGRGGAGRGQ QRFAPLNSWP
     DNVGLDKARR LIWPVKQKYG RKISWADLIV LTGNVALESM GFKTFGFAGG REDSWEPDED
     VYWGMESTWL DDKRYSGDRQ LETPLAAVQM GLIYVNPEGP NGNPDPLASA RDIRETFARM
     AMNDEETVAL IAGGHTFGKT HGAGDASHVG PEPEAAPLEQ MGLGWKSSFG SGKAGDAIGS
     GLEVIWTSTP TQWSNNFFWN LFGYDWELTK SPAGAHQWQP KGGAGADSVP DPFEPGKRRV
     PTMLTSDIAL RADPTYEKIS RRFFENPNEF AEAFARAWFK LTHRDMGPRV RYLGPEVPSE
     ELLWQDPIPM PDHPQVDEQD VSALKAKVLA SGLSVSELVS TAWASASTFR GSDKRGGANG
     ARVRLAPQKD WEVNQPAQLA TVLEVLGALQ VEFNRAATGG KQVSLADLIV IAGNAGVEQA
     AAAAGVEITV PFTPGRGDAS AEQTDVDSMA VLEPIADGFR NYLKGAYTIP AEKLLIDKAQ
     LLSLSAPEMT VLIGGLRVLG TNVGDSKHGV FTDRREVLTN DFFRNLLDMG TEWKPTSEAN
     EAYEGRDRAT GELKWLASRV DLVFGSHSQL RALSEVYGSE DSQQKFVRDF VAAWTKVMNA
     DRFDIKHN
 
 
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