ID C9SL18_VERA1 Unreviewed; 481 AA.
AC C9SL18;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Vanillyl-alcohol oxidase {ECO:0000313|EMBL:EEY19386.1};
GN ORFNames=VDBG_05495 {ECO:0000313|EMBL:EEY19386.1};
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};
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DR EMBL; DS985219; EEY19386.1; -; Genomic_DNA.
DR RefSeq; XP_003004382.1; XM_003004336.1.
DR AlphaFoldDB; C9SL18; -.
DR GeneID; 9531369; -.
DR KEGG; val:VDBG_05495; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_024402_0_1_1; -.
DR OMA; NVPTIRH; -.
DR OrthoDB; 5474593at2759; -.
DR Proteomes; UP000008698; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 2.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748:SF114; ARYL-ALCOHOL OXIDASE VANILLYL-ALCOHOL OXIDASE (AFU_ORTHOLOGUE AFUA_3G09500)-RELATED; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT DOMAIN 64..261
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 481 AA; 53763 MW; 8A321DB4327ED7C4 CRC64;
MPHAQPRRLP PGFTSEDFAA FVKAIIPIVG DENFSIVSAD VELKDGDYVN PCKAHDMHAV
YDKEFFVSCA VVHPRTVTEV QEIMRLCNKM QMPVWPYSVG RNTGYGGAAP RVPGTLGMEL
GRHMNRIHEV NVDGAYALVE PGVTFFSLYD HLVKTGLDEQ LWLDVPDLGG GSIIGRHQSD
FYHFMMHCGM EVVLPDGTLV RTGMGSLPDP ASRNSNLSAD QQPPNKAWQL FNYGFGPYND
GLFTQSSLGI VVKMGVWLMP NPGGYQAYMI TFPRDEDLGA IVDIIRPLRL QMVLQNVPTI
RHILLDAAVA GDKASYTDKT SPLSGDELDA IAAKLDLGRW NFYGAVYRRF AEAGLDFIGT
FTIGMREMHH IVCVVFNRED PQQRLRARWL TRQLIKDCAE HGWGEYRTHL ALMDQIAGTY
NFNNSSQMKL NETIKNALDP NGILAPGKNG IWPAKYDKRA WVLEKDEADK LLFAGIPMTR
L
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