位置:首页 > 蛋白库 > KATG2_BURCJ
KATG2_BURCJ
ID   KATG2_BURCJ             Reviewed;         736 AA.
AC   Q4F6N6;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
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}; Synonyms=katA;
GN   OrderedLocusNames=BceJ2315_55450; ORFNames=BCAM2107;
OS   Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS   NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=216591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=17371508; DOI=10.1111/j.1574-695x.2007.00224.x;
RA   Charalabous P., Risk J.M., Jenkins R., Birss A.J., Hart C.A., Smalley J.W.;
RT   "Characterization of a bifunctional catalase-peroxidase of Burkholderia
RT   cenocepacia.";
RL   FEMS Immunol. Med. Microbiol. 50:37-44(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX   PubMed=18931103; DOI=10.1128/jb.01230-08;
RA   Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA   Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA   Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA   Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA   Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA   Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT   "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT   cystic fibrosis patients.";
RL   J. Bacteriol. 191:261-277(2009).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. Shows peroxidase specificity towards odianisidine,
CC       ABTS and pyrogallol, but methoxyphenol and 2-chloronaphthol are not
CC       peroxidized. {ECO:0000255|HAMAP-Rule:MF_01961,
CC       ECO:0000269|PubMed:17371508}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5 for the peroxidase reaction and 6.0 for the
CC         catalase reaction. Active from pH 5.5 to 8.5.
CC         {ECO:0000269|PubMed:17371508};
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; DQ112341; AAZ14051.1; -; Genomic_DNA.
DR   EMBL; AM747721; CAR55964.1; -; Genomic_DNA.
DR   RefSeq; WP_006490370.1; NC_011001.1.
DR   AlphaFoldDB; Q4F6N6; -.
DR   SMR; Q4F6N6; -.
DR   STRING; 216591.BCAM2107; -.
DR   PeroxiBase; 2309; BcenCP01_J2315.
DR   EnsemblBacteria; CAR55964; CAR55964; BCAM2107.
DR   KEGG; bcj:BCAM2107; -.
DR   eggNOG; COG0376; Bacteria.
DR   HOGENOM; CLU_025424_2_0_4; -.
DR   OMA; KWTATRM; -.
DR   OrthoDB; 49441at2; -.
DR   BioCyc; BCEN216591:G1G1V-6173-MON; -.
DR   BRENDA; 1.11.1.6; 8982.
DR   Proteomes; UP000001035; Chromosome 2.
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   1: Evidence at protein level;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT   CHAIN           1..736
FT                   /note="Catalase-peroxidase 2"
FT                   /id="PRO_0000354740"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         268
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..227
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   253)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        227..253
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   91)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   736 AA;  80487 MW;  48CC314FEA9C30A3 CRC64;
     MSNEGQCPFN HANGGGTTNR DWWPNELRLD LLSQHSSKTD PLDPGFNYAE AFNSLDLDAL
     RKDLAALMTD SQDWWPADFG HYGPLFVRMA WHSAGTYRMG DGRGGAGRGQ QRFAPLNSWP
     DNVSLDKARR LLWPIKQKYG QKISWADLLI LTGDVALTTM GFKTFGYAGG REDTWEPDRD
     VYWGSETTWL GGDLRYDKGG ACESQHGGNA GRNLENPLAA VQMGLIYVNP EGPDGNPDPV
     AAAYDIREVF GRMAMNDEET VALIAGGHAF GKTHGAGPAD NVGLEPEAAG LEQQGLGWKN
     SFGTGKGADT ITSGLEVTWS DTPTQWGMGF FKNLFGYEWE LTKSPAGAHQ WVAKNAEPTI
     PHAHDPSKKL LPTMLTTDLS LRFDPVYEKI SRHFMDNPDV FADAFARAWF KLTHRDMGPR
     ARYLGPDVPT EELIWQDPIP AVDHVLVDDT DVAPLKETIL ASGLSVAELV STAWASASTF
     RGSDKRGGAN GARIRLAPQK DWAVNEPARL AKVLKVLERI QGEFNSTQPG GKKISLADLI
     VLAGGAGIEQ AAKRAGHDVV VPFAPGRMDA SQEQTDAHSF AVLEPVADGF RNFVKGKFAV
     PAEALLIDKA QLLTLTAPQM TALVGGLRVL NVQTGDEKHG VFTDQPETLT VDFFRNLLDM
     ATEWKPIAGE DTYEGRDRRT GELKWTGTRV DLVFGSNAVL RALSEVYASA DGEAKFIRDF
     VAAWVKVMNL DRFDLA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024