ID A0A165AYF9_EXIGL Unreviewed; 720 AA.
AC A0A165AYF9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:KZV79533.1};
GN ORFNames=EXIGLDRAFT_464555 {ECO:0000313|EMBL:KZV79533.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV79533.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV79533.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV79533.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; KV426597; KZV79533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165AYF9; -.
DR STRING; 1314781.A0A165AYF9; -.
DR InParanoid; A0A165AYF9; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552:SF115; DEHYDROGENASE XPTC-RELATED; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..720
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007855430"
FT DOMAIN 684..720
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 637..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 720 AA; 75983 MW; CED0F3BB98DEC2BB CRC64;
MAPCTRLVGL LAFTTVAFGY ADVLSDLAAR QITARQAKSS YDYIVVGAGQ AGVVIAARLS
EDSSKSVLLV EYGYIDNTPS QIEPSSATSY AQRNLYNLTA VVQPGLNNVA NSTVYAAAVV
GGGSTINGMM LDRAAPLDYD NWYTCPALLS TVTEAFSTSR AKLNNSGWGF NDLLPYFKKS
MQLTPPRSDI ASDFNITYDL SAYGSNSPIQ LSYPTYQYPG TKIQYQGIIQ AGVAPQKEGG
LNGYGLFWYP GALDPVKVQR SYAVNGYYTP VASRSNLQLL TGYRVNEVQF DSSKRATGVT
IQARGTPDGQ NVQVVGATTE VVLTAGYLHT PQILQRSGVG AASLLQRANI PVVVDLPGVG
SNFQDHASAS ASWRFATDAN PNPTSLYTNT TFMQWADQLW AANRTGPRSM GVGNVGAWIP
LSVLASDSSS IISQVQAQNA SQYLPSTYTP ELLAGFQAQR DLLVTSYGSL QAGVIELPFS
GSGSASLSLE HPLSRGTITI NTSNKYAEPV VDYQTFVNPV DPLIVARSFT FVRKWMNTTA
MRQLSPSETS PGSTLTTDAQ LISAARSGTR ASTAHGCCTA PMQPRNLGGV VGPDLLVYGV
TGLSVGDISI IPLIPAAHTC ATVYGIAEKA ADLIKARAGS TPPPSSSTST SGTTSSTTTT
TTSTTTTRTT TTTTTTTTSV PTGCVSQKWG QCGGIGWTGC TACASGSTCQ KQNDYYSQCL
//
