ID   C9SQN4_VERA1            Unreviewed;       563 AA.
AC   C9SQN4;
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 dehydrogenase {ECO:0000313|EMBL:EEY21159.1};
GN   ORFNames=VDBG_07269 {ECO:0000313|EMBL:EEY21159.1};
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|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS985222; EEY21159.1; -; Genomic_DNA.
DR   RefSeq; XP_003002698.1; XM_003002652.1.
DR   AlphaFoldDB; C9SQN4; -.
DR   STRING; 526221.C9SQN4; -.
DR   GeneID; 9527703; -.
DR   KEGG; val:VDBG_07269; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_6_3_1; -.
DR   OMA; PSMMNHE; -.
DR   OrthoDB; 3215324at2759; -.
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:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 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; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008698};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..563
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003002535"
FT   DOMAIN          67..90
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          258..272
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         217
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         496..497
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   563 AA;  61381 MW;  350B0B0C856BCCA5 CRC64;
     MLSSTLPVAV ALLGIQAALG RPIQGLDRAE IEEAYDFIIA GGSAIDWRFD TVPQEGLDGK
     ILTYYRGRGL GGSSAINGFY YGRGTSTVYD RWQDLGNPGW SWADVYPLFI KGTHFNPQDE
     TKGFDNTYKT WDPSAYSDGP LEIAYQGFVP PTGIAFMHAC EAANIPIVHD YNTGNSTGVK
     QGTATLDANL LRSSSYDGYL KKAINRTNLD VLYYAPVQSL LWDTEGEKPR ATGVQFLDHP
     SGRMYQVHAA KEVVVSMGAF QTPQLLMVSG VGPAAELEKF GIEPVYINEN VGQHLDDHSV
     FSIMATVADE FSTSQYADFD LLQAIQEEFY TNGTGVYTAP SGITNGFQRL PEEELRDIGA
     GAVVDAGLSD QSHIEYLFES IFYPGGPTPF YTPLANESYI SLTASSMVAL SRGNITLRGT
     SMSAAPNINP NYYTHDADRA IAIQAFKYLR KILAHPELAK FTYGPDNGEV SPGAAVSSDD
     DDAIFEYVKA NTIPNWHASG TARMRREDDG GVVDARLKPY GIDGLRIVDC SIIPVLPDVN
     IVGPVFMIGE KGAQLIREDY DDC
//