ID   KATG2_ALKMQ             Reviewed;         416 AA.
AC   A6TV07;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Catalase-peroxidase 2;
DE            Short=CP 2;
DE            EC=1.11.1.21;
DE   AltName: Full=Peroxidase/catalase 2;
DE   Flags: Precursor;
GN   Name=katG2; OrderedLocusNames=Amet_3934;
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:0000250}.
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;
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   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. The N-terminus is much
CC       shorter than in related proteins and lacks the active sites and the
CC       heme-binding sites. Moreover, the 71 first amino acids of this sequence
CC       are not homologous to other KatG sequences. {ECO:0000305}.
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DR   EMBL; CP000724; ABR50025.1; -; Genomic_DNA.
DR   RefSeq; WP_012064979.1; NC_009633.1.
DR   AlphaFoldDB; A6TV07; -.
DR   SMR; A6TV07; -.
DR   STRING; 293826.Amet_3934; -.
DR   PeroxiBase; 3625; AmeCP02_QYMF.
DR   PRIDE; A6TV07; -.
DR   EnsemblBacteria; ABR50025; ABR50025; Amet_3934.
DR   KEGG; amt:Amet_3934; -.
DR   eggNOG; COG0376; Bacteria.
DR   HOGENOM; CLU_025424_3_0_9; -.
DR   OrthoDB; 49441at2; -.
DR   Proteomes; UP000001572; Chromosome.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
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   InterPro; IPR000763; Catalase_peroxidase.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   PANTHER; PTHR30555; PTHR30555; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   SUPFAM; SSF48113; SSF48113; 2.
PE   5: Uncertain;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..416
FT                   /note="Catalase-peroxidase 2"
FT                   /id="PRO_0000354719"
SQ   SEQUENCE   416 AA;  46834 MW;  01ACF81E6638AD38 CRC64;
     MLLPLIVFLL SVLIHHRIYS SFFLHFYSPQ YYMICSRLTL LSSCSWHDFH LKLILLEFAS
     QSTNPVPALH NDPTYEKISR RFHENPEAFA DVFARAWFKL LHRDMGPQTR YLGPEVPEEE
     LIWQDPIPAV DYELTDAEIA ELKAKILDSG LTVSDLVTTA WASASTFRGS DMRGGANGAR
     IRLAPQKDWE VNQPEQLTKV LTVLEDIQNQ LDKKVSIADL IVLGGSAAIE KSAQDAGFDV
     TVPFALGRGD ATQEQTDIES FEVLEPISDG FRNYQKKQYS VSAEELLLDK AQLLNLTAPE
     MTVLVDGMRV LGTNYNGTQH GVFTDRVGTL TNDFFVNLLD MGVEWKPMDG GLYEARNRKT
     GEVVRTATRV DLVFGSNSVL RALVEVYAQD DNKEKFVGDF IAAWIKVMNA DRFDLD