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KATG_ALIB4
ID   KATG_ALIB4              Reviewed;         735 AA.
AC   A8EV24;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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};
GN   Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Abu_1548;
OS   Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Arcobacteraceae; Aliarcobacter.
OX   NCBI_TaxID=367737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM4018;
RX   PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA   Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA   Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A.,
RA   Rogosin A., Stanker L.H., Mandrell R.E.;
RT   "The complete genome sequence and analysis of the Epsilonproteobacterium
RT   Arcobacter butzleri.";
RL   PLoS ONE 2:E1358-E1358(2007).
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; CP000361; ABV67797.1; -; Genomic_DNA.
DR   RefSeq; WP_012013181.1; NC_009850.1.
DR   AlphaFoldDB; A8EV24; -.
DR   SMR; A8EV24; -.
DR   STRING; 367737.Abu_1548; -.
DR   EnsemblBacteria; ABV67797; ABV67797; Abu_1548.
DR   KEGG; abu:Abu_1548; -.
DR   eggNOG; COG0376; Bacteria.
DR   HOGENOM; CLU_025424_2_0_7; -.
DR   OMA; MILAGNC; -.
DR   OrthoDB; 49441at2; -.
DR   Proteomes; UP000001136; 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; 1.
PE   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Reference proteome.
FT   CHAIN           1..735
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354721"
FT   ACT_SITE        96
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         264
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            92
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        95..223
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   249)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        223..249
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   95)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   735 AA;  81448 MW;  5459DB4B5E9D6BC0 CRC64;
     MAGKCPMGFG TTNPMVRNGG TSNKDWWPNQ LNLKILSQHS NKVNPLGSDF DYAKEFSKLD
     YDALKADLTA LMTDSQDWWP ADYGHYGPLF IRMAWHSAGT YRTGDGRGGA STGSQRLAPL
     NSWPDNANLD KARRLLWPIK QKYGNKISWA DLMILAGNVA LESMGLKTFG FSGGRVDVWE
     PEEDIYWGKE AQWLATSDKE NSRYSGDRDL ENPLAAVQMG LIYVNPEGPD GVPDPIKSGI
     DIRETFARMA MDDEETVALT AGGHTFGKCH GAGDAANVGA EPEAEGLVAQ GLGWLSKFLS
     GKGDDTITSG IEGSWTANPT RWDNEYFDIL LSYDWELTKS PAGAWQWIPK NPKEEHLAPA
     AHDKTKKVTT IMTTADMAMK MDPIYAKISK RFHENPQEFA DAFARAWFKL THRDLGPKSK
     YIGPEIPKED LIWQDPIPPI NYEIIDEKDI EILKEKLLSS SLGVSKLVSL AWASASTYRD
     SDKRGGANGA RIALEPQRSW ESNSYLNLDE SLKILETIKG EFNSSNSNKK VSLADLIVLG
     GCAAVEKAAK DAGFNIKVPF TAGRADATQE QTHVESFSHL EPIADGFRNY SKAKYTLSTE
     ELLIDKAQLL SLTIPEMIVL VGGMRVLGAN YANSDLGVFT SNVGVLSNDF FVNLLDMKTA
     WYPTTQEEDS FVGKDRQSGS MKYSASRVDL LFGSNSQLRA VSEVYAQEDS KEKFVQDFIN
     AWTKVMNLDR FDIKK
 
 
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