ID A0A137NUQ8_CONC2 Unreviewed; 360 AA.
AC A0A137NUQ8;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:KXN66487.1};
DE Flags: Fragment;
GN ORFNames=CONCODRAFT_11665 {ECO:0000313|EMBL:KXN66487.1};
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:KXN66487.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN66487.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN66487.1,
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 -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; KQ964720; KXN66487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137NUQ8; -.
DR STRING; 796925.A0A137NUQ8; -.
DR EnsemblFungi; KXN66487; KXN66487; CONCODRAFT_11665.
DR OMA; FESHYFI; -.
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; 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 PANTHER; PTHR11552:SF213; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000070444};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..360
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007294072"
FT DOMAIN 307..321
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT NON_TER 360
FT /evidence="ECO:0000313|EMBL:KXN66487.1"
SQ SEQUENCE 360 AA; 39617 MW; FB5FCA071CFCBFE9 CRC64;
MIYKLIFSAI LCLVKCDDEV FDYIVVGSGP GGSIAALELA RRGFTTLLIE AGSNISNNNI
TTPGLGTRTW DDESIAWNFR VDYNDHSPDK RKNVLYPRAS AIGGCANHNG MANLFPRAHG
FDRLVEATGD PSFGESTFAK YFESILLDSP PPTDPKIDRR FLTLSTDKLS GVKEDPKDKY
IGKAIEEAVA HETAHQTAND KLAIGTAENE FESHYFIPNN IDRKVTPPVR RGPRRAVNEE
LAKNPKLTVW TESLVTKIIL EGNVAKGVEY MPGAHLYRAS PVARRENKAA PAIKKVYARK
EIVVSGGTFN TPQIMMLSGI GDSNELKALG IEPKVHLPGV GKNLRDHIEV GVIWELNSDY
//
