ID A0A0D2BMN2_9EURO Unreviewed; 548 AA.
AC A0A0D2BMN2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=PV05_06204 {ECO:0000313|EMBL:KIW53791.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW53791.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW53791.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW53791.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; KN847320; KIW53791.1; -; Genomic_DNA.
DR RefSeq; XP_013314375.1; XM_013458921.1.
DR AlphaFoldDB; A0A0D2BMN2; -.
DR STRING; 348802.A0A0D2BMN2; -.
DR GeneID; 25328112; -.
DR HOGENOM; CLU_017779_4_1_1; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
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; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT DOMAIN 116..295
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 60766 MW; E6A9ACDB17DDDBA4 CRC64;
MSGSASKGLA RVLRQAKRPS IARTRPSQCI PTSYEPMRTF SVTPRRREDT AEPHHNVRYT
TDMYNIKRDA KFSEITPDHI QFFKSTLGDD AAVVDGVTKD ASDDLEAFNT DWMKKYRGHT
KLVLKPKSTE EVSKVLKYCN DNKLAVVPQG GNSGLVGGSV PVFDEIVISL SRMNNIRSFD
DVSGILVVDG GVILEVADNF LAGHNHLFPL DLGAKGSCQI GGNVATNAGG LRLLRYGSLH
GNVLGLEAVL PDGTIVDDLS KLRKNNTGYD LKQLFIGGEG TIGIITGVSV QCPQRSKAVN
VAYFGLPSFE HVQKAFKEAK IQLGEILSAF ELMDSQSQGF VHRVTGNKRP LEGDHPFYCL
IETSGSNTEH DNEKLEKFLE YVMGEEIVSD GVLAQDETQV KALWAWREGI TEAIGHYGGT
YKYDLSIPLA ELYKLVEETR ERLTSMNLIG DDDSHPAIGV VGYGHMGDSN LHLNVPVRRY
TKEVEEAIEP WVYEWIQKRN GSISAEHGLG IAKKKYIGYS RSETMIKLMK QIKNLYDPNG
IMNPYKYI
//
