ID   C9SWQ2_VERA1            Unreviewed;       606 AA.
AC   C9SWQ2;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Alcohol oxidase {ECO:0000313|EMBL:EEY23443.1};
GN   ORFNames=VDBG_09553 {ECO:0000313|EMBL:EEY23443.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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; DS985228; EEY23443.1; -; Genomic_DNA.
DR   RefSeq; XP_003000358.1; XM_003000312.1.
DR   AlphaFoldDB; C9SWQ2; -.
DR   STRING; 526221.C9SWQ2; -.
DR   GeneID; 9528062; -.
DR   KEGG; val:VDBG_09553; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_5_1_1; -.
DR   OMA; IMRRTKM; -.
DR   OrthoDB; 2392848at2759; -.
DR   Proteomes; UP000008698; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF78; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000008698}.
FT   DOMAIN          282..296
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         96
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         235
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         538..539
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   606 AA;  66421 MW;  761220576800AA43 CRC64;
     MGVYTKLADD IDEVDVIIAG GGTAACVVAG RLAEADPKLS ILVIEGGQDN RGVSNIENPA
     FFLDHLLPTS KTAIFYKGNK SEQCAGREVI VPSGGVLGGG SSINFMMYTR AQRSDFDSWK
     SPGWSADEIL PFLKKLETYH GPGDKSRHGD SGPVHISSGT FRSEFSESEF IKATGEVGWP
     EIKDLQTLDA NNGIERWLRY VSPEGKRQDS ARVYLHDKMD NDKYPNLHIL TQSKVVRVLL
     DDDKRAVGVE YTPNPDFQAV LETTKHPKKQ VKARQLVVVS CGACGTPPVL ERSGLGDPEI
     LKKAGVDVKV DLPGVGRDYQ DHQLILYPYL SSLKEHETID GMLRNPDKRQ ELIDKKDPRV
     GWKSIDISSK LRPSDDDVSA LGPEFQDAWN KDFKNAPDRP LMLMGLVSCF LGDPASVPEA
     GYVTVGTYTA YPYSRGHMHI TGPEVSDALD FDPGYLSDAH DIDLKKQLWA YKKQREIMRR
     TAMFRGELAA GHPAFAEGSA AACAAVESAL SDVKDIEYSA EDDKAIEQWI RENVGTTWHS
     IATAKMAPRE ENGVVDHDLN VWGTKGLKIA DLSIPPMNVG ANTNNTALVV GEKAADIIIR
     ELGLSV
//