ID A0A0D2BKI5_9EURO Unreviewed; 469 AA.
AC A0A0D2BKI5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=PV08_00015 {ECO:0000313|EMBL:KIW19443.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW19443.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW19443.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW19443.1,
RC ECO:0000313|Proteomes:UP000053328};
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 spinifera CBS89968.";
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 oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; KN847492; KIW19443.1; -; Genomic_DNA.
DR RefSeq; XP_016239659.1; XM_016374383.1.
DR AlphaFoldDB; A0A0D2BKI5; -.
DR STRING; 91928.A0A0D2BKI5; -.
DR GeneID; 27327098; -.
DR VEuPathDB; FungiDB:PV08_00015; -.
DR HOGENOM; CLU_018354_10_0_1; -.
DR OrthoDB; 1068078at2759; -.
DR Proteomes; UP000053328; 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:UP000053328}.
FT DOMAIN 41..212
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 469 AA; 50573 MW; 259DA8D188A08860 CRC64;
MGSTGALTPS FDELRSSLKA SVVFTPDSEG YQESLHRWSE AAEKRAAVVV QVTTAEDAST
AVLSAQANGL EIAVVGGGHS TSGSSSTEGG LVVDLTKMRQ VTVDVEKKTI KAGGGCIWED
VDHAAAEYGL ATVGGTVNHT GVGGLTLGGG YGWLTGKYGL TIDNLLEVEV VTADGQILTA
SETENPDLFW ALRGAGQSFG VATSFTFQGY KQSNPVWGGL LVFKTSDLDK VLNFANKLVI
NTKGESGMVV GFGAPAPKRK AAVLTILFYD GPKSEALRYY ADLFALGPIK DLTSEIPYKE
VNSMLNRVST HGDRKTQKGS AFTVPLPEHL GQLILDDYLK FMAEIPDAIK TIILFEFFSQ
RKVNEVSQTA MSFANRGEHY NILFSTRWVG AQNDKTCREW TRNMASKVDK ELAKHKNNDG
VGQYGNYDGI ASASAKDIFG VNYERVLALK KQYDPNNVFK KGAGKFPIE
//
