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KATG_ALTMD
ID   KATG_ALTMD              Reviewed;         766 AA.
AC   B4RW28; F2G4D5;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   03-AUG-2022, entry version 83.
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};
DE   Flags: Precursor;
GN   Name=katG {ECO:0000255|HAMAP-Rule:MF_01961};
GN   OrderedLocusNames=MADE_1016605;
OS   Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS   ecotype).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1774373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX   PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA   Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA   Johnson J., Friedman R., Rodriguez-Valera F.;
RT   "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT   Alteromonas macleodii suggests alternative lifestyles associated with
RT   different kinds of particulate organic matter.";
RL   ISME J. 2:1194-1212(2008).
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; CP001103; AEA99445.1; -; Genomic_DNA.
DR   RefSeq; WP_012519733.1; NC_011138.3.
DR   AlphaFoldDB; B4RW28; -.
DR   SMR; B4RW28; -.
DR   PeroxiBase; 7308; AmacCP01.
DR   EnsemblBacteria; AEA99445; AEA99445; MADE_1016605.
DR   KEGG; amc:MADE_1016605; -.
DR   HOGENOM; CLU_025424_2_0_6; -.
DR   Proteomes; UP000001870; 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   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..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CHAIN           27..766
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354720"
FT   ACT_SITE        123
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         285
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            119
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        122..244
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   270)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        244..270
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   122)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   766 AA;  84458 MW;  DB68CFA186110ADF CRC64;
     MNMNRFRKTT LSALVALSLG ATGAIANDQI SKPAGAKGTG MTKAFQPKSN QFWWPDQLDL
     SPLRDHDNRS NPLGEDFDYA KAFSKLDLDQ VKSDINELLT TSQDWWPADF GNYGPFFIRL
     SWHSAGTYRT LDGRGGGDGG QMRFDPLNSW PDNGNLDKAR RLLWPIKQKY GESLSWGDLM
     ILAGTVGMEN MGFDTYGFAG GRTDDWEPDM VYWGPEVEML ASDREEREGK LQRPLGATHM
     GLIYVNPEGP KGVPDPMGSA KNIRTAFARM AMNDEETVAL IAGGHTFGKM HGAHKPADCL
     EAEPGGAGLE EQGLGWKNNC GKGNAEDTVT SGLEGAWTQL PTKWTSLYLQ NLLGFEWKQT
     RSPAGAIQWV PTDESLHTSV PDAHVEGKKN PPVMTTADLA LKYDPEYRKI AERFLADPKE
     YQTAFAKAWF KLTHRDMGPK ERYLGNDIPR ENFIWQDPVP KADYKTISDK DVKKLKADIL
     DSGLTVQQLV KTAWAGASSF RASDLRGGAN GARIALEPQM SWEANEPETV KAVVAKLKEL
     QEDYNSRMFS KKKVSLADLI VIGGAAAIEK AAADAGVEVS VPVVPGRTDA TQEQTDVNSF
     SLLEPTADAF RNYYNAEASY RSPTDMLVDK ADQLNLTVPE MTVLLGGLRS LGANTGGTNH
     GVFTDNVGTL NNDFFVTLLD MGVKWRKTDD ASVYEGVNRS TGEVMYTGTP VDLVFGSNSE
     LRAVAEVYAY DNAKTRFVED FVDAWTKVMT LDRFDLRHDL NAKLAK
 
 
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