ID A6R651_AJECN Unreviewed; 749 AA.
AC A6R651;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
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 ORFNames=HCAG_05109 {ECO:0000313|EMBL:EDN08610.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN08610.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|EMBL:EDN08610.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NAm1 {ECO:0000313|EMBL:EDN08610.1};
RA Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDN08610.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NAm1 {ECO:0000313|EMBL:EDN08610.1};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Henn M.,
RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E., Brockman W., Rounsley S., Young S., LaButti K., Pushparaj V.,
RA DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA Pearson M., Howarth C., Larson L., Luoma S., White J., Yandava C.,
RA Kodira C., Zeng Q., Oleary S., Alvarado L., Taylor J., Sil A., Goldman B.;
RT "Annotation of the Ajellomyces capsulatus (Histoplasma capsulatum)
RT genome.";
RL Submitted (SEP-2005) 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; CH476659; EDN08610.1; -; Genomic_DNA.
DR AlphaFoldDB; A6R651; -.
DR STRING; 339724.A6R651; -.
DR VEuPathDB; FungiDB:HCAG_05109; -.
DR HOGENOM; CLU_010645_3_0_1; -.
DR OMA; WQMSDRA; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000009297; Unassembled WGS sequence.
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 3: Inferred from homology;
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009297}.
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; 84695 MW; 0F961178284E9BC4 CRC64;
MTSKVAEGLQ RVKELVENMQ PGEQKVVDLA RDTTDVNGCL PFTTDHGVKV SDTDFWLRLA
SENQTGPSLL EDQIAREKIH RFDHERIPER VVHARGTGAF GHFKLYESAA DVTSAGVLTD
TSRTTPVFVR FSTVQGSKGS FDTVRDVRGF ATKFYTEEGN WDLVGNNIPV FFIQDAVKFP
DFVHAVKPEP HNEVPQGQTA HNNFWDFVYM HPEATHMFMW AMSDRAIPRS YRMMQGFGVN
TFVLVNKQGK RHFVKFHWMP ELGVHSLVPD ESFKLGGQDP DFHRKDLMEA IDNKVYPKWK
LGIQVLPEEK EHDFDFDILD STKIWPETLI PVRYVGEMEL NRNIDEFFPQ TEQVAFCTAH
IVPGIEFSDD PLLQGRNFSY FDTQITRLGV NWEELPINRP VCPVMNHNRD GAMRHKITQG
TVNYWPNRFE ACPPTKPEDG GFVTYPQKVE QSIKVRMLSS KFREHINQAQ LFYNSLSEYE
KLHVKNAFCF ELDHCDDPIV YNRLVSRISE IDHALAQAVA VKVGAPTPQR PGRDNPGQTA
INLSQKYIND RQPSSPTMKG RRIAILIGDG YDSVAFGTAI AAVSAMGALP FIIGTKRQPI
FADDEDRNHS KGVTPNHNYT SQRSTCFDAT FIPGGSHIKE LSQLGPIQHW VAEQFGHCKA
IGATGEAINL IVQALNNLPD LEVASASSGH PVDWYGVVTS SKLHEPHSLT EGIKLFPEAS
DFLGKFFYQI SQHRNYEREM AGLTDKVPF
//
