ID A2QH45_ASPNC Unreviewed; 338 AA.
AC A2QH45;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Contig An03c0180, genomic contig {ECO:0000313|EMBL:CAK38315.1};
GN ORFNames=An03g05540 {ECO:0000313|EMBL:CAK38315.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK38315.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK38315.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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DR EMBL; AM270059; CAK38315.1; -; Genomic_DNA.
DR RefSeq; XP_001390434.1; XM_001390397.1.
DR AlphaFoldDB; A2QH45; -.
DR EnsemblFungi; CAK38315; CAK38315; An03g05540.
DR GeneID; 4980543; -.
DR KEGG; ang:An03g05540; -.
DR VEuPathDB; FungiDB:An03g05540; -.
DR HOGENOM; CLU_037263_0_1_1; -.
DR OrthoDB; 35622at2759; -.
DR Proteomes; UP000006706; Chromosome 6R.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR CDD; cd03190; GST_C_Omega_like; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR047047; GST_Omega-like_C.
DR InterPro; IPR016639; GST_Omega/GSH.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR32419:SF23; GLUTATHIONE S-TRANSFERASE (EUROFUNG); 1.
DR PANTHER; PTHR32419; GLUTATHIONYL-HYDROQUINONE REDUCTASE; 1.
DR Pfam; PF13410; GST_C_2; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR PIRSF; PIRSF015753; GST; 1.
DR SFLD; SFLDG01206; Xi.1; 1.
DR SFLD; SFLDG01148; Xi_(cytGST); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 35..139
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13409"
FT ACT_SITE 36
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
FT ACT_SITE 179
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
SQ SEQUENCE 338 AA; 38534 MW; FF99CD824013A776 CRC64;
MSIHQAGTAD GWHGIVPSTA FPAEPDRYHL YIGHFCPFAH RVNIVRHLKG LTDLIKVSVV
RAYPKGDLKG WPGWKFPASD DEYPGATVDH LYGEDYLHKV YFRADPEYKG RYSVPLLWDT
KTGTAVCNES LEMLRWLPKA FNSQISPSLA EIDLYPSHLQ AKIDAISPWM QSDVNSGVYK
AGFTDSQEEY NDKVVRVFGA LNKLERIIAQ NGGPFVLGKE MTELDVMLYT TLIRFDVVYV
EHFKCNLGTI RHDYPVLHNW LKGMYWDVEA ARDTTDFKHI KENYTKSHWH INPRAITPLG
PCPDIEEGVE RDWTKLRVGG VKHPAVLEHE ASIPDLSQ
//
