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KATG1_ALKMQ
ID   KATG1_ALKMQ             Reviewed;         730 AA.
AC   A6TNI2;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Catalase-peroxidase 1 {ECO:0000255|HAMAP-Rule:MF_01961};
DE            Short=CP 1 {ECO:0000255|HAMAP-Rule:MF_01961};
DE            EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE   AltName: Full=Peroxidase/catalase 1 {ECO:0000255|HAMAP-Rule:MF_01961};
GN   Name=katG1 {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Amet_1570;
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF;
RX   PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
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; CP000724; ABR47750.1; -; Genomic_DNA.
DR   RefSeq; WP_012062788.1; NC_009633.1.
DR   AlphaFoldDB; A6TNI2; -.
DR   SMR; A6TNI2; -.
DR   STRING; 293826.Amet_1570; -.
DR   PeroxiBase; 2533; AmeCP01_QYMF.
DR   PRIDE; A6TNI2; -.
DR   EnsemblBacteria; ABR47750; ABR47750; Amet_1570.
DR   KEGG; amt:Amet_1570; -.
DR   eggNOG; COG0376; Bacteria.
DR   HOGENOM; CLU_025424_2_0_9; -.
DR   OMA; MILAGNC; -.
DR   OrthoDB; 49441at2; -.
DR   Proteomes; UP000001572; 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..730
FT                   /note="Catalase-peroxidase 1"
FT                   /id="PRO_0000354718"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        96
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         259
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..218
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   244)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        218..244
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   95)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   730 AA;  80734 MW;  4B07364EE570C052 CRC64;
     MQEKGKCPVT GMTKHKTSGG TTNQDWWPNQ LNLKMLHQNP TMRNPMGERF NYAEEFKKLD
     FEALKNDLYA LMTDSQEWWP ADYGHYGPLF IRMAWHSAGT YRMGDGRGGA GTGNQRFAPL
     NSWPDNVNLD KARRLLWPIK QKYGKKISWA DLMILAGNCA LESMGFKTFG FAGGREDIWE
     PEEDIYWGQE NEWLGDKRYS GDRELENPLA AVQMGLIYVN PEGPNGQPSA LASGKDIRDT
     FARMAMNDEE TVALVAGGHT FGKCHGAGSA THVGPEPEAA NIEEQGLGWK NSMGSGKGIH
     TISSGIEGAW TPTPIKWDNS YLDTLFNYDW DLVKSPAGAW QWVPTDPTAA DSVPDAHDPS
     KRHAPMMTTA DLALRMDPIY GPIAKGFREN PEAFADAFGR AWFKLTHRDM GPRTRFLGPE
     VPTEELIWQD PVPAVDFELI DEDDITGLKG KIIDSGLSLS ELVSTAWASA SSFRGSDKRG
     GANGARIRLA PQKDWEVNQP EQLQTVLQAL EKIQDTFNSA QSGKKRISLA DLIVLAGCAG
     VEQAAKNAGF DVCVPFTPGR TDASQEQTEV ESFSVLEPMA DGFRNYSKGK YTISAEKLLV
     DRTQLLGLTA PEMTVLVGGM RVLNANYNKS QQGVLTKRPE NLTNDFFVNL LDMDTAWKVT
     AEGGDMFEGI DRKTGELKWT GTGVDLVFGS NSELRAIAEV YASDDAKQKF VEDFVTAWNK
     VMNADRFDLA
 
 
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