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Database: UniProt
Entry: G7XWP5_ASPKW
LinkDB: G7XWP5_ASPKW
Original site: G7XWP5_ASPKW 
ID   G7XWP5_ASPKW            Unreviewed;       490 AA.
AC   G7XWP5;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:GAA91354.1};
GN   ORFNames=AKAW_09468 {ECO:0000313|EMBL:GAA91354.1};
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA91354.1};
RN   [1] {ECO:0000313|EMBL:GAA91354.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA91354.1};
RX   PubMed=22045919; DOI=10.1128/EC.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000256|ARBA:ARBA00004913}.
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329}.
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DR   EMBL; DF126480; GAA91354.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7XWP5; -.
DR   STRING; 1033177.G7XWP5; -.
DR   VEuPathDB; FungiDB:AKAW_09468; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   InParanoid; G7XWP5; -.
DR   Proteomes; UP000006812; 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:0009820; P:alkaloid metabolic process; 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; IPR002226; Catalase_haem_BS.
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; PS00437; CATALASE_1; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism {ECO:0000256|ARBA:ARBA00022589};
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          7..395
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        57
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         340
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   490 AA;  55163 MW;  9E43FBF05EE3D20B CRC64;
     MSKPVYTLAE GQPLPNPSVS TTLPTFGGGA ITTLGDTLLI ETLTHFNRER IPERVVHAKG
     NGAWGEFRVT KDISHLTHAK FLNGVGKTTK VLFRASTTGG EKGSADTVRD VHGFSVKFFT
     EEGNHDIVGN HVPVFFVRDP VRFPSLNRSH KRHPTTGLPD MNMYWDFHSN QPESVHTLMH
     VFGSRGLPQS ARRMTGFGIH TFKLVGHDGK FRYCKFHFRP VLGSHNFTPE EATRMAGVNP
     DFHNEDLFQA ILRGDYPKWK FYIQVMEPEQ AETYGRAVFD ITKVWPHKDF PLIEVGEMTL
     NRNPENFFAE IEQAAFSPSN LVPGIAVTPD PMLQARMFAY PDAQRYRLGV NYTQLPPNRA
     ICPVYAPYER DGLATMGRNY GGDPNYIKST LTPGVFSQSV QEVRHHEWLR SGAVLGLNEI
     PVDDEDFVQP RALWNNVFDE TERSLWVDNV AGALEGVVPE IQKATIAMFS RVEPQIGQRL
     EAKLKSSSRL
//
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