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Database: UniProt
Entry: A0A066XJF7_COLSU
LinkDB: A0A066XJF7_COLSU
Original site: A0A066XJF7_COLSU 
ID   A0A066XJF7_COLSU        Unreviewed;       558 AA.
AC   A0A066XJF7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Putative vanillyl-alcohol oxidase {ECO:0000313|EMBL:KDN69328.1};
GN   ORFNames=CSUB01_05725 {ECO:0000313|EMBL:KDN69328.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN69328.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDN69328.1}.
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DR   EMBL; JMSE01000528; KDN69328.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066XJF7; -.
DR   STRING; 1173701.A0A066XJF7; -.
DR   eggNOG; KOG1231; Eukaryota.
DR   HOGENOM; CLU_024402_0_0_1; -.
DR   OMA; FNDNAQM; -.
DR   OrthoDB; 5474593at2759; -.
DR   Proteomes; UP000027238; 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; 1.
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:UP000027238}.
FT   DOMAIN          65..267
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   558 AA;  61989 MW;  F5295D1C73795BA6 CRC64;
     MASVEDPIVL PPNFTPELFQ NFIVRAQDIC GVENVRVVPK DKPLEGDSYL NQPKSHDHFP
     LYEKTKFVAS AVVTPRHVPD VQALVALCNE LVMPVWPISL GRNFGYGGAS PRVPGSVVMD
     LGHHMNRILE VNVEGAYVLL EPGVSFRDLY EHMEKHDLLE HLWLSVPVGQ GSVLGNAIER
     GVGATPYGDH WGMHCGMEVV LPNGKLVRTG MGGVPNPNAD PNVRPDEQPG NETWQLFNTG
     YGPYNDGLFS QSNLGIVTKI GMWLMPSPGG YQPYEITFEN DSDLPEIVDI IRPLRLQMVL
     QNMPVLRHTL LNAAHCGPKS KWTATEGPVS EEEVDTIAKR LDMGRWQLIG AVYGPKLVRD
     ALLNVIRHEF LSIPGSRFFL PEDRARDSPL RARELLMQGI PTVEELRCLD WLPNGGQLLW
     APISKVSGED AKKQHDVAKN LIISHGFDYL GAFAVGMREL HHVVGIPYRL DVPEDVTKVR
     QLAHKLIKET TAHGWGQSRA HTALMDPVAE AFNWNDNAQM QLNETIKNAL DPNGIIAPGK
     NGVWPASYDK KKWVLDGN
//
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