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
//