ID A0A137PAV1_CONC2 Unreviewed; 591 AA.
AC A0A137PAV1;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Alcohol oxidase {ECO:0000313|EMBL:KXN72062.1};
DE Flags: Fragment;
GN ORFNames=CONCODRAFT_48094 {ECO:0000313|EMBL:KXN72062.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN72062.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN72062.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN72062.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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}.
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DR EMBL; KQ964461; KXN72062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137PAV1; -.
DR STRING; 796925.A0A137PAV1; -.
DR EnsemblFungi; KXN72062; KXN72062; CONCODRAFT_48094.
DR OMA; EDPCVDR; -.
DR OrthoDB; 3382025at2759; -.
DR Proteomes; UP000070444; 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; 2.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 2.
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:SF213; DEHYDROGENASE, PUTATIVE-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 Pfam; PF05834; Lycopene_cycl; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000070444};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..591
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007294628"
FT DOMAIN 239..351
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 454..586
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT BINDING 258
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:KXN72062.1"
FT NON_TER 591
FT /evidence="ECO:0000313|EMBL:KXN72062.1"
SQ SEQUENCE 591 AA; 65823 MW; F3CB3C77CA2F71E5 CRC64;
MQFLNFIASL TSIYVSFGTV SAQQNSYDYI VVGAGPTGSM VATELARKGF STLLIDAGKD
YMHPNITVPA FQFNTLETEQ IQWDYWVKHY DESTGLRQKV LYPKASGLGG CTLHNSLIHV
YPNSRDFKEM VELTGDKSWA ETTFRKYLET IALYRLGSSD RRWLPLSNLN VFRILDLDPK
LLGLAKLILG PFFDSITGFD PNGYAGKGKL NTDFETDFLP KSNVDELSTG VPFRRGIAEY
LKTRRNDPKL TIWTETLVTK VILDGNKATG VEFAKGAHLY RASPIARRED KPLPNLESVY
ARKEVIISAG TFNSPQLAML SGIGHKDELA AVGIESKVHL PGVGKNLHDR YEISVNFEFD
SDLKLLDGCL FKADRKADPC YAKYLDYGIG PYSVAGYLSA KSLKSDPSLP EPDMVHFNFP
LNFTGYHPGT PAQAAGSHRA FSFLNLKAHG FNRAGVLRLE SNDPRDTPYI NFRYFEQGAD
KDIPAIIKGI KDIRKTMAKT SLRYKEVRPG AQVTSDAALE DYIRKTSWGH HATGTMKIGK
NDDPNAVLDG NFKVRGVENL RVIDLSVMPN LPGYFPVMFL YLLGMKGADV I
//
