ID A0A074WZJ5_9PEZI Unreviewed; 701 AA.
AC A0A074WZJ5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:KEQ75202.1};
GN ORFNames=M436DRAFT_41749 {ECO:0000313|EMBL:KEQ75202.1};
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:KEQ75202.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ75202.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ75202.1,
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 -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; KL584705; KEQ75202.1; -; Genomic_DNA.
DR RefSeq; XP_013429580.1; XM_013574126.1.
DR AlphaFoldDB; A0A074WZJ5; -.
DR STRING; 1043004.A0A074WZJ5; -.
DR GeneID; 25409618; -.
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; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR47190:SF5; PX DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000027730};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..701
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001701829"
FT DOMAIN 105..128
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT REGION 589..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 73839 MW; E2C3B2B65D10E360 CRC64;
MSWLLPFLLL PALGVSAQTA SPSYDYIVAG AGPAGIIVAQ RLAESGASVI LLERGNASTF
SRGGRDILPW NNTVTQYDVP GVRHYIKTSF ADKSEYCTDT AGNAGCVLGG GTMVNQLAYI
PPQNLDFDDK WPAGWKWADV ASAAERVHAR NPGSTCPSAD GVHYDQTSYT AFANFFDTQG
YKSVDAIAEP NSKHNVYSHA PYSVKDGLVA GPVLTYLPLA QALPNFKLQL HTKVIRVVRQ
RSIVSGVEVE VVGQRQIINV SASGRVILAS GVFSTPRILF NSGIGPNDQL QIVASSASTN
NVTLPPSSDW INLPVGQGIK DHAIVTLNFN TTGLVDFLDT PYFISPSSNV IDMYSHGTGI
LTQGYQRFTM WTSNTTSDGS VRFFQGTCYA SGQNQVSMKL YLTHGITSSG VLSITPAGNT
VYSVDPYLNT AEDKYALASF IDNLLVQTRK TGSSLIYAGS PADTGASLSK VFTGGSHWVS
TAKMGIDDGR INNGTSVVDL ELKIYGTDNL FVVDASMHPD LPTGNLQATV QVAAEAAAAR
ILALPKQSFL STSSVLGATK GSSVSTSSSD DVITSSSSIA TTLSTVVPSS SVSSVGSSTT
SSSNTADPTN PTCPSSNSTT FVAKSGAVFL IECYMDRAGH DMASVNVPSN RIADCINKCD
ALTGCVDISM SGTACYMKSA VGGRVVQSKY VRGARKINGS I
//
