ID A0A0A1T428_9HYPO Unreviewed; 545 AA.
AC A0A0A1T428;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Putative Choline oxidase {ECO:0000313|EMBL:CEJ80074.1};
GN ORFNames=VHEMI00279 {ECO:0000313|EMBL:CEJ80074.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ80074.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ80074.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(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; CDHN01000001; CEJ80074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1T428; -.
DR STRING; 1531966.A0A0A1T428; -.
DR HOGENOM; CLU_002865_7_1_1; -.
DR OrthoDB; 3714148at2759; -.
DR Proteomes; UP000039046; 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; 3.30.410.40; -; 1.
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; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF152; OXIDASE (CODA), PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04090)-RELATED; 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; PS00624; GMC_OXRED_2; 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:UP000039046}.
FT DOMAIN 264..278
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 545 AA; 60110 MW; B9E5A2D5EADA6837 CRC64;
MTTQALPPNA ANAFDYIIVG GGTAGCVLAS RLSSYLPEKK VLVIEGGPSD FNLNQVLNLR
EWLTLLGGDL DYDYPTTAQP NGNSHIRHSR AKVLGGCSSH NTLISFRPFR HDMDRWVAQG
CKGWTFENVT RHIDNLRNTF QPVHARHRNQ LCKDWVQACS DAFNIPVISN FNEEIRETGK
LTQGAGFFNV SYNPDDGKRS SASVAYIHPI LRGEERRPNL TILTEAWVSK VLVENDAATG
IVVTLKSGQT LTLRPRKEII LSAGAVDTPR LMLHSGLGPR AQLEGLGIPV VKDIRGVGEN
LVDHPETIIM WELNKPVPAN QTTMDSDAGI FLRREAHNAA GNDADAADIM MHCYQIPFTL
NTGRLGYREV PDQYAFCMTP NIPRPRSRGR IYLTSADPSV KPALDFRYFT DPEGYDAATL
VAGIKAARKV AEQAPFKDWL KEEVAPGPKV QTDEAISEYA RRAAHTVYHP AGTTKMGDVA
KDEFAVVDSE LKVRGIKNLR IADAGVFPEM PSINPMLTVL AIGERAAEMI AMEEGWKLDA
NKSRL
//
