ID   CATB_AJECA              Reviewed;         728 AA.
AC   Q9Y7C2;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Catalase B;
DE            EC=1.11.1.6;
GN   Name=CATB;
OS   Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=5037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 26032 / G217B;
RX   PubMed=11932457; DOI=10.1099/00221287-148-4-1129;
RA   Johnson C.H., Klotz M.G., York J.L., Kruft V., McEwen J.E.;
RT   "Redundancy, phylogeny and differential expression of Histoplasma
RT   capsulatum catalases.";
RL   Microbiology 148:1129-1142(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 26032 / G217B;
RA   Johnson C.H., McEwen J.E.;
RT   "Characterization of the Histoplasma capsulatum gene for the externally
RT   located catalase B enzyme.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen peroxide.
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=1.11.1.6;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; AF139985; AAD33062.1; -; mRNA.
DR   EMBL; AY103480; AAM53417.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y7C2; -.
DR   SMR; Q9Y7C2; -.
DR   PRIDE; Q9Y7C2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
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   CDD; cd03132; GATase1_catalase; 1.
DR   Gene3D; 1.20.1370.20; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR043156; Catalase_clade2_helical.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR041399; Catalase_large_C.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   PANTHER; PTHR42821; PTHR42821; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF18011; Catalase_C; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF56634; SSF56634; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   2: Evidence at transcript level;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Secreted.
FT   CHAIN           1..728
FT                   /note="Catalase B"
FT                   /id="PRO_0000084914"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         394
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   728 AA;  80818 MW;  B63DFAB3BA015D0E CRC64;
     MRSLKLILAS ASVVSATCPY MSGEMPNSQN GPLDRRHDTL SDPTDQFLSK FYIDDEQSVL
     TTDVGGPIED QHSLKAGNRG PTLLEDFIFR QKIQHFDHER VPERAVHARG AGAHGVFTSY
     NNWSNITAAS FLNAAGKQTP VFVRFSTVAG SRGSVDSARD IHGFATRLYT DEGNFDIVGN
     NVPVFFIQDA IQFPDLIHAV KPQPDSEIPQ AATAHDTAWD FFSQQPSSLH ALFWAMSGHG
     IPRSMRHVDG WGVHTFRLVT DEGNSTLVKF RWKTLQGRAG LVWEEAQALG GKNPDFHRQD
     LWDAIESGRY PEWELGFQLV NEADQSKFDF DLLDPTKIIP EELVPFTPIG KMVLNRNPKN
     YFAETEQIMF QPGHVVRGID FTDDPLLQGR LYSYLDTQLN RHGGPNFEQL PINRPRIPFH
     NNNRDGAGQM FIPLNTAAYT PNSMSNGFPQ QANRTHNRGF FTAPGRMVNG PLVRELSPSF
     NDVWSQPRLF YNSLTVFEKQ FLVNAMRFEN SHVRSETVRK NVIIQLNRVD NDLARRVALA
     IGVEPPSPDP TFYHNKTTVP IGTFGTNLLR LDGLKIALLT RDDGSFTIAE QLRAAFNSAN
     NKVDIVLVGS SLDPQRGVNM TYSGADGSIF DAVIVVGGLL TSASTQYPRG RPLRIITDAY
     AYGKPVGAVG DGSNEALRDV LMAAGGDASN GLDQPGVYIS NDVSEAYVRS VLDGLTAYRF
     LNRFPLDR