ID A0A074XSA4_9PEZI Unreviewed; 544 AA.
AC A0A074XSA4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:KEQ77451.1};
DE Flags: Fragment;
GN ORFNames=M436DRAFT_17587 {ECO:0000313|EMBL:KEQ77451.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ77451.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ77451.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ77451.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; KL584702; KEQ77451.1; -; Genomic_DNA.
DR RefSeq; XP_013431509.1; XM_013576055.1.
DR AlphaFoldDB; A0A074XSA4; -.
DR STRING; 1043004.A0A074XSA4; -.
DR GeneID; 25407966; -.
DR HOGENOM; CLU_011025_2_1_1; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000027730; Unassembled WGS sequence.
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 Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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; PTHR47190:SF2; CELLOBIOSE DEHYDROGENASE (AFU_ORTHOLOGUE AFUA_2G17620); 1.
DR PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000027730}.
FT DOMAIN 92..115
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 259..273
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 94
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 221
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 513
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 524..525
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KEQ77451.1"
FT NON_TER 544
FT /evidence="ECO:0000313|EMBL:KEQ77451.1"
SQ SEQUENCE 544 AA; 58700 MW; 415CEE6797706863 CRC64;
AGDSAFDYIV VGSGPGGVTV ADKLSESGAS VLLVERGQAT TGQWNGNNRP QWLDNTGMTF
YDVPALDDQI WTKGGDFTND IFCPDIVGGI SGCVLGGSGA INSGLWWKPT TWDWDTMFPE
KWNSTNMANV TERVFSRLPG TEVPSQDGKL YYQQGADVIE GALHAANWTL VSANEVPNQK
DRVYSNTTFM FQDGERSGPM SVYLGSAYPR PNFSLYTNAI VDRVIREGSK ITGVEISNTA
ADGFRGTVKA NKAVVLAAGA FGTPKVLMRS GIGPKDQLET VRNAEGSKMI NEDQWIDLPV
GYNLMDNINT DIVISQPDVV YYDFAGLWNS PNQGDVDAYL NGRTGMLAQS ASNLNPMIWE
MLNGTNGLQG LQWTARVDTS LDIPNDNKHN MVLAQYITLG QAARGRTTIT SDLKMNVSTG
VSIMEHESDQ IAIAQGIETM VNILKSVPGL EVLSPPSGMS ALDYVKSTTH LYVNHWLGSC
KMGNDDGRKE NGTAVVDADS KVYGTDNLFI ADGSIFPGQT TSNPQAAITI VGERVAELIL
ALNQ
//
