ID B8N244_ASPFN Unreviewed; 470 AA.
AC B8N244;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=Catalase, putative {ECO:0000313|EMBL:EED56166.1};
GN ORFNames=AFLA_034380 {ECO:0000313|EMBL:EED56166.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED56166.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED56166.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329}.
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DR EMBL; EQ963473; EED56166.1; -; Genomic_DNA.
DR RefSeq; XP_002374948.1; XM_002374907.1.
DR AlphaFoldDB; B8N244; -.
DR STRING; 332952.B8N244; -.
DR EnsemblFungi; EED56166; EED56166; AFLA_034380.
DR VEuPathDB; FungiDB:AFLA_001311; -.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_2_0_1; -.
DR OMA; QERMVWH; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
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 CDD; cd08157; catalase_fungal; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024711; Catalase_clade1/3.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF26; CATALASE 2; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038928-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559}.
FT DOMAIN 21..367
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT BINDING 312
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:PIRSR038928-2"
SQ SEQUENCE 470 AA; 53280 MW; CE472B462DA6D060 CRC64;
MAERYYTLAE ATALPFNCGT TLVADFLCSK IHNSLRLSPI SLVREFPSEW STPRRRAGKK
SPVLLRVSTV GPEAGSADTT RDVHGWAMKI YTDEGNLDWV FNNTPVFFVR DPIKFPSLNR
SHKRHPTTHL PDANMFWDFH VGNPEGIHEL LHLFSDRGTP KSIRHMNAYS GHTYKLTKED
GSFKYVKFHI KTAQGVKNMT AEESLKIAGE DPDYLIRDMF EAIEKGDYPV WNVYVQVMDP
ADAEKYRWNI FDMTKVWSHK DYPLRQIGKL TMNRNPKNYF TDIEQAAFSP STMVPGIAPS
ADPMLQARMF AYPDAARYRL GVNYQQLPTN AAKAPVYCPY QRDGAMRFDD NYGGDPNYVG
SSLQPTKFYQ EVKNSGAARL SGLTEHEKWV GEVTNFQSHI TDDDFVQPAA LWEVIGREPG
HQDRTIANLS GHIKNVRSPQ LRNAVYELFA KVNADLGERL KKATEAAVSA
//
