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KATG2_BURCM
ID   KATG2_BURCM             Reviewed;         741 AA.
AC   Q0B385;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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};
DE   Flags: Precursor;
GN   Name=katG2 {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Bamb_5842;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 3 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-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; CP000442; ABI91388.1; -; Genomic_DNA.
DR   RefSeq; WP_011660735.1; NC_008392.1.
DR   AlphaFoldDB; Q0B385; -.
DR   SMR; Q0B385; -.
DR   STRING; 339670.Bamb_5842; -.
DR   PeroxiBase; 2702; BamCP02.
DR   PRIDE; Q0B385; -.
DR   EnsemblBacteria; ABI91388; ABI91388; Bamb_5842.
DR   GeneID; 44696389; -.
DR   KEGG; bam:Bamb_5842; -.
DR   PATRIC; fig|339670.21.peg.6795; -.
DR   eggNOG; COG0376; Bacteria.
DR   OMA; EEIFWGP; -.
DR   Proteomes; UP000000662; Chromosome 3.
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;
KW   Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CHAIN           29..741
FT                   /note="Catalase-peroxidase 2"
FT                   /id="PRO_5000128247"
FT   ACT_SITE        108
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            104
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        107..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                   107)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   741 AA;  80910 MW;  7BDB180568080277 CRC64;
     MQKKRVGKSV VAALAIIAMS AGTVAAWADG APRTNDFWWP ERLDLSPLRQ HDVESNPYGK
     DFDYAQAFNK LDIEAVKKDI RATLTTSQDW WPADYGNYGP FFIRMAWHGA GTYRTYDGRG
     GAGGAQQRFE PLNSWPDNAN LDKARRLLWP IKKKYGENIS WGDLMVLTGN VALESMGFQT
     FGFGGGREDD WQSDLVYWGA GTKFMSNNRD KNGKLEKPLA ATQMGLIYVN PEGPNGNPDP
     VAAAKDIRDA FGRMAMNDEE TLALIAGGHT FGKAHGAASP DKCVGAAPAG AGVEAQGLGW
     ANKCGTGKGA DTITSGLEGA WSVDPVHFTM QYLDNLLEHD WVLTKSPAGA HQWMPKDAQD
     IVPDAHDPSK RHPLMMFTTD IALKVDPAYS AIAKRFHAHP EEFKLAFAKA WFKLTHRDLG
     PKARYLGKDV PKVDLIWQDP LPVAGYQMIG DADIAELKRR ILASGVPKAE LIKTAWASAA
     SFRATDYRGG ANGARIRLAP ENDWAVNDPA SLSKVLKSLE GIQSGFNRNR TDGKQVSLAD
     LIVLGGSAAV EDAARKAGYD VKVPFSPGRV DATQAQTDVA SFAVLEPTAD GFRNYYQKSN
     ERSPAELMVD RASKLDLTVP EMTVLVGGLR ALDANAGHSR LGVLTNRPGT LSNDFFVNLL
     DMSTQWTKSS SADGTYEGRD RKTGALKWTA SPVDLVFGSS SELRAVAEVY ASDDAHEKFV
     RDFVQAWTKV MNLDRFDLKR S
 
 
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