ID E4V6Q2_ARTGP Unreviewed; 483 AA.
AC E4V6Q2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=6-hydroxy-D-nicotine oxidase {ECO:0000313|EMBL:EFQ96768.1};
GN ORFNames=MGYG_08692 {ECO:0000313|EMBL:EFQ96768.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; DS989831; EFQ96768.1; -; Genomic_DNA.
DR RefSeq; XP_003169145.1; XM_003169097.1.
DR AlphaFoldDB; E4V6Q2; -.
DR STRING; 535722.E4V6Q2; -.
DR GeneID; 10024390; -.
DR VEuPathDB; FungiDB:MGYG_08692; -.
DR eggNOG; ENOG502SKWA; Eukaryota.
DR HOGENOM; CLU_018354_10_0_1; -.
DR InParanoid; E4V6Q2; -.
DR OMA; RSSPHYE; -.
DR OrthoDB; 541418at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
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; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002669}.
FT DOMAIN 64..237
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 52597 MW; F1CDBF6790A1E703 CRC64;
MLDSAPFSST AEHRQEPTPF DPAVDAQGSE PIIQTLTTLD SALKLYTRSS PHYESLRGCF
NKLITARPLV ICRPVTIEQV QLIVRAVSDL PAGNECPPLA VRGGGHDVWG RGCIADSVTI
DVRELDQARL AEDKQSVTAG GGILSGNLVG FLNNHGLCTS NGTAADVGWT GWAVWGGYGP
FNDYLGLGVD NILAAKVVLA DGRLVEAKPE SELLWAIRGA GGNFGVIVEV TVKVYHMPTI
LGGFIVYKWE ETEQALHRTQ ELLDKGVPDA LGIQVGFNRS RVGLGMSLIY TWADSNDLDE
GKKWLETLKQ LATVVVDTTT ETTFKDFQAM TTKPFKDPID VCTRSISIPR FTPETIAILL
KYAEDIPIGG RYNVVSHVGH GKGTKPNNST CFGTREPHIL FHINAPVPDG AGGMERAQAW
VDGLMADIKG TGQALKPVYV SFMGKDEETQ NSFGQNWKRL QELKGTLDKR DLFRFAQPML
GKM
//
