ID A0A074VYF6_9PEZI Unreviewed; 620 AA.
AC A0A074VYF6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE SubName: Full=Choline dehydrogenase-like protein {ECO:0000313|EMBL:KEQ65850.1};
GN ORFNames=M437DRAFT_63394 {ECO:0000313|EMBL:KEQ65850.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ65850.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ65850.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ65850.1,
RC ECO:0000313|Proteomes:UP000030672};
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; KL584826; KEQ65850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074VYF6; -.
DR STRING; 1043003.A0A074VYF6; -.
DR HOGENOM; CLU_002865_6_1_1; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000030672; 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 Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 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; PTHR11552:SF115; DEHYDROGENASE XPTC-RELATED; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 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.
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:UP000030672};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..620
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001701004"
FT DOMAIN 115..138
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 301..315
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 554
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 597
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 264
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 620 AA; 67601 MW; FED3B4E774BBD0B7 CRC64;
MAPVFSSLTR LTAVISSVLL LSADVVLGTT TREQTLTGTY DYIIVGGGVS GLVVANRLSE
KAQKSVLVLE YGYNDNSTKT LWPYYGTAYN DPDMFEINST PQENLQNQTF VAYAGKVLGG
GSIVNGMGYD RGTQPDYDAW GELGNDGWDW SNLLTYFKKS STFTPNKKET LDKYNYTYDL
SAYGNGPVQV SLPEWQYPEM PAFWDAMEEM KINKVQEGAL GEPGHFWVPA STDPKYQTRS
SARSAYYDPI ASRPNLKVVT GVQVQEIVFA TLTAKGVKLL DRDTGKTYTA YADMELILAA
GAIHTPQILQ LSGVGPASVL KEAGLKVKVD LPGVGNNFQD HPAAYLMWNF NNDTTPNTNS
LTNNATFNAT SYDEYVANKT GPYTQAHGNG AAFLPLSKIA PDTYKTIANK LASQEAADYL
PAIYSDYPEL VAGYEAQRKI QVQQFNSDNA SMYEFSFQGG GFAITALQKP TSRGTVYINP
KNPYGEPIID YHGLQNPVDM DLLLASIRYT RQIYNTSALS VFEPVELTPG TKYQTDDELK
SQIASGLVLP TFAHPASSCA MMPRDLGGVV DSGLQVYGIK KVTIVDASIM PLIPGTHLQA
TVYAVAEKAA DIIKARHGAL
//
