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Database: UniProt
Entry: A0A177E224_ALTAL
LinkDB: A0A177E224_ALTAL
Original site: A0A177E224_ALTAL 
ID   A0A177E224_ALTAL        Unreviewed;       645 AA.
AC   A0A177E224;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   03-MAY-2023, entry version 22.
DE   SubName: Full=Alcohol oxidase {ECO:0000313|EMBL:OAG25019.1};
GN   ORFNames=CC77DRAFT_1037281 {ECO:0000313|EMBL:OAG25019.1};
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:OAG25019.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG25019.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG25019.1,
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   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; KV441470; OAG25019.1; -; Genomic_DNA.
DR   RefSeq; XP_018390440.1; XM_018527057.1.
DR   AlphaFoldDB; A0A177E224; -.
DR   STRING; 5599.A0A177E224; -.
DR   GeneID; 29112651; -.
DR   KEGG; aalt:CC77DRAFT_1037281; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_1037281; -.
DR   OMA; KGWVKLR; -.
DR   OrthoDB; 3382025at2759; -.
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; 2.
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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF80; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000077248}.
FT   DOMAIN          341..355
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   645 AA;  69814 MW;  0BA69B6A4DE7C9C0 CRC64;
     MRFSNRTHGS NDTYDYIVVG SGPGGGPLAV NLAKAGFKTL LLEAGDDESA EKRTQALALS
     EVPIPANLGW SFWVRHYDDD EQTKRYQRLT WRLPNGDLWV GPGSSAPAGA EMLGVQYPRG
     ATLGGSTLVN AGFNILPSER DWSQIEALTG DSSWNPERMR EIFAKTEKNL YLPRGTPGHG
     FDGYLQLNEG NGTVFTTSPQ SSEIYRSLVS EVGQNPDELE QLFDTDPNQL RSDRDQTVGL
     FGGVFHANGT WGRYSVRDHV LATLRAVDAT GRKRYPLEVR LNSLASKVLF EDSINGTAPR
     AIGIEYLEGK SIYQGDLRYN ASNNATTKQV YASKEVIVSG GTFNTPQLLL LSGIGSAADL
     EALNITVVAD LPGVGRNMQD HNEIATIGLA AQNISVDGGS GFPRSQCTPR APNDPCYDLW
     QQGQGPYAEG SIMGSMFFLK TNHSSTGERD IGMWSGPVGV RGFWPQTPNQ SFVDPPNTFG
     FHTVHMHGSN RAGYVKLRSA DPTAQPEINF RHFSDEGADQ DIAAIKEAVA FFRRVHAGVV
     APVGPNEVIW PTCSGSVSAD GTCSDEGNDE QFIRDNNYGH HATSTSSIGS DDDPNAVLDS
     KFRVRGVEGL RVVDASAFPR APGAFPVLAV FMLSEKAALD ILSTQ
//
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