ID Q9UUT2_AJECA Unreviewed; 749 AA.
AC Q9UUT2;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 03-MAY-2023, entry version 112.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN Name=CATA {ECO:0000313|EMBL:AAF01462.1};
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 {ECO:0000313|EMBL:AAF01462.1};
RN [1] {ECO:0000313|EMBL:AAF01462.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11932457;
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] {ECO:0000313|EMBL:AAM53416.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G-217B {ECO:0000313|EMBL:AAM53416.1};
RA Johnson C.H., McEwen J.E.;
RT "Characterization of the differentially expressed CATA gene of Histoplasma
RT capsulatum.";
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 {ECO:0000256|RuleBase:RU004142}.
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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:0000256|PIRNR:PIRNR038927,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|PIRNR:PIRNR038927,
CC ECO:0000256|RuleBase:RU000498}.
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DR EMBL; AF189368; AAF01462.1; -; mRNA.
DR EMBL; AY103479; AAM53416.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UUT2; -.
DR PeroxiBase; 5216; AcapKat01.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
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 Gene3D; 2.40.180.10; Catalase core domain; 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; IPR002226; Catalase_haem_BS.
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; CATALASE; 1.
DR PANTHER; PTHR42821:SF1; CATALASE-B; 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; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 2: Evidence at transcript level;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927}.
FT DOMAIN 43..433
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 93
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 166
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 380
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:0000256|PIRSR:PIRSR038927-2"
SQ SEQUENCE 749 AA; 84644 MW; 64E4B262D314276F CRC64;
MTSKVEEGLQ RVKELVENMQ PGEQKVADLA RDTTDVNGCL PFTTDHGVKV SNTDFWLRLA
SENQTGPLLL EDQIAREKIH RFDHERIPER VVHARGTGAF GHFKLFESAA DVTSAGVLTD
TSRTTPVFVR FSTVQGSKGS FDTVRDVRGF ATKFYTEEGN WDLVGNNIPV FFIQDAVKFP
DFVHAVKPEP HNEVPQGQTA HNNFWDFVYM HPEATHMFMW AMSDRAIPRS YRMMQGFGVN
TFVLVNKQGK RHFVKFHWMP ELGVHSLVPD ESFKLGGQDP DFHRKDLMEA IDNKVYPKWK
FGIQVLPEEK EHDFDFDILD PTKIWPESLI PVRYIGEMEL NRNVDEFFPQ TEQVAFCTAH
IVPGIEFSGD PLLQGRNFSY FDTQITRLGV NWEELPINRP VCPVMNHNRD GAMRHKITQG
TVNYWPNRFE ACPPTKPEDG GFVTYPQKVE QSIKARMLSS KFREHINQAQ LFYNSLSEYE
KLHVNNAFCF ELDHCDDPIV YNRLVSRISE IDHALAQAVA VKVGAPTPPR PGRDNPGQTT
INLSQKYIND RQLSSPTIKG RRIAILIGDG YDSVAFGTVI AAVSAMGALP FIIGTKRQPI
FADDEDRNHS KGVTPNHNYT SQRSTCFDAT FIPGGSHIKE LSQLGLIQHW VAEQFGHCKA
IGATGEAINL IVQALSNLPD LEVASASSGH PVDWYGVVTS SKLHEPHSLT EGIKLFPEAS
DFLGKLFYQI SQHRNYEREM AGLTDKVPF
//
