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KATG3_MYCS2
ID   KATG3_MYCS2             Reviewed;         744 AA.
AC   A0QYP1; I7FN10;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Catalase-peroxidase 3 {ECO:0000255|HAMAP-Rule:MF_01961};
DE            Short=CP 3 {ECO:0000255|HAMAP-Rule:MF_01961};
DE            EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE   AltName: Full=Peroxidase/catalase 3 {ECO:0000255|HAMAP-Rule:MF_01961};
GN   Name=katG3 {ECO:0000255|HAMAP-Rule:MF_01961}; Synonyms=katG;
GN   OrderedLocusNames=MSMEG_3729, MSMEI_3640;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK74103.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AFP40103.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000480; ABK74103.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001663; AFP40103.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_888029.1; NC_008596.1.
DR   AlphaFoldDB; A0QYP1; -.
DR   SMR; A0QYP1; -.
DR   STRING; 246196.MSMEI_3640; -.
DR   PRIDE; A0QYP1; -.
DR   EnsemblBacteria; ABK74103; ABK74103; MSMEG_3729.
DR   EnsemblBacteria; AFP40103; AFP40103; MSMEI_3640.
DR   KEGG; msg:MSMEI_3640; -.
DR   KEGG; msm:MSMEG_3729; -.
DR   PATRIC; fig|246196.19.peg.3673; -.
DR   eggNOG; COG0376; Bacteria.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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   Reference proteome.
FT   CHAIN           1..744
FT                   /note="Catalase-peroxidase 3"
FT                   /id="PRO_0000354840"
FT   ACT_SITE        107
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            103
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        106..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                   106)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   744 AA;  82295 MW;  A980D38FD8FCBF8E CRC64;
     MPESPDAYVN RTYDQTVAVR RSLKRRNSPA ASEDGLGWPR RLNLRILAQP CRTSSPLGED
     FDYAKEFLSL DLDELARDID EVLTTSQDWW PADFGHYGPL VLRMAWHFAG TYRIGDGRGG
     AGAGMLRFAP LNSFPDNRNL DKARRLLWPV KKKYGRKISW SDLMIFAGNR ALESMGCRTF
     GFAGGREDAW EADETYWGPE STWLADERHS GVRDLDQPLA ASEMGLIYVD PQGPATLPDP
     LASARDIRET FRRMGMNDEE TVALIAGGHT FGKSHGPTDP SRCLGPEPEG APLEALGLGW
     VNSFGTGNGA DTVTSGLDGI WTATPTKWDM SFLTTLFAYE WDVALSPAGM WQWVPRNGAG
     AGTVPDPYDP SRTHAPTMLT TDLALQEDPR YRVIALRFLE NPDEFADTFA RAWFKLTHID
     MGPIQRYLGP LVPTERMIWQ DPVPHVDHEL ADADDVAALK REILGSGLSV SQLVTTAWAS
     ASTFRNSDKR GGANGARIRL EPQRSWAVNE PEKLAIVLDR LERIRRRFND SHRGGKQISA
     ADLIMLGGCA AVEHAAAEAG HPIEVPCRLG RTDAPQEWTD IEWFSALEPT ADAFRNYVGE
     GNRPPPEHLL VDRASQLTLT APQMTVLLGG LRVLGANHGG SPLGVFTASP GALSNDFFVN
     LLDVNIEWTP RADTADWTAA YEGRDRRTGE VTWIASRVDL SFASDPVLRA ISEVYASADA
     EEKFVRDFVS AWDKVMNLDL FDRT
 
 
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