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Database: UniProt
Entry: A0A177DTU6_ALTAL
LinkDB: A0A177DTU6_ALTAL
Original site: A0A177DTU6_ALTAL 
ID   A0A177DTU6_ALTAL        Unreviewed;       618 AA.
AC   A0A177DTU6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Alcohol oxidase {ECO:0000313|EMBL:OAG22209.1};
GN   ORFNames=CC77DRAFT_791550 {ECO:0000313|EMBL:OAG22209.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG22209.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG22209.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG22209.1,
RC   ECO:0000313|Proteomes:UP000077248};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; KV441475; OAG22209.1; -; Genomic_DNA.
DR   RefSeq; XP_018387630.1; XM_018533195.1.
DR   AlphaFoldDB; A0A177DTU6; -.
DR   GeneID; 29118789; -.
DR   KEGG; aalt:CC77DRAFT_791550; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_791550; -.
DR   OMA; DYMSVPQ; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000077248; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552:SF210; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G00610)-RELATED; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077248}.
FT   DOMAIN          289..303
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         99
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         250
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   618 AA;  67495 MW;  156F8111E4737366 CRC64;
     MVQHTGCVTS IDALSTQEPD FIVIGGGIGG LVVANRLSED AEKKVLLIEA GANRRGDPKI
     DTVGMLSTLY GDPDYDWDFM TEPQMHVNGR QIPHPRGKVL GGSSAINFGA TVYPSKADFE
     SWEALGNEGW GATGVAPYLR KFSRFTAPSA ETKELLSIDY INEELHGKDG PVPVTIPDVY
     GPFQASWVKT LDNLGWCNSD DPIEGEKLGT FACGLSIDAE TKTRGYAASA YYTQQVAERP
     NLEVLTETFV EKILTNVCDG SVQAIGVKIR TRSGVHEITA KKEVILSAGT IQSPQVLELS
     GIGQKELLEK HGIPVVLDSP GVGENLQDHA ISAPCFEIAD DQFSADIMRD PNIVQAVLQQ
     YMSTKTGPLV GIPISVTMLP LIDSDGRVSH DEIAQMARQC GEDKDLPLWQ KRQYEQLEKQ
     ISGPNEAAGY AMMLPLQLNI SAGATQMKEL LAPSNPKNFI TIMAVNNHPF SRGFCHIRSA
     DPKEKPILDP KYLSHPLDLE ILARYTQYIE TIVKTEPFAS LLKPSGRLPD GKRATDLDAA
     KDIVKERLLS TFHPTGTCAM MPKELNGVVD SRLKVHGTKN LRIVDASIFP METLGNIQAT
     VYAVAEKAAD LIKQDWKK
//
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