ID F0UQF1_AJEC8 Unreviewed; 567 AA.
AC F0UQF1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:EGC47941.1};
GN ORFNames=HCEG_07156 {ECO:0000313|EMBL:EGC47941.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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; DS990640; EGC47941.1; -; Genomic_DNA.
DR AlphaFoldDB; F0UQF1; -.
DR STRING; 544711.F0UQF1; -.
DR VEuPathDB; FungiDB:I7I53_10045; -.
DR HOGENOM; CLU_002865_6_1_1; -.
DR OMA; EHAMGNA; -.
DR Proteomes; UP000008142; 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; 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; 2.
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:UP000008142}.
FT DOMAIN 249..263
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 501
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 544
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 210
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 567 AA; 61979 MW; C51FDDC4E3D86C49 CRC64;
MLLSFLPSGS RARTLCYALI LFASFATSSV LVRDGDKQSL RDRNEFDYII VGGGLTGLVA
AHRLSENLFG MAYDRASAAD YDSWEALGNR GWGWKGMFPY FRKSADFTPP KKAVVNKYGY
TYDESAYGRF GPLQVTFPDW QVPDQYKMAG AFTELGVAHL REHAMGNAVG QFWAPATIDA
KTMTRSSSLT AYYDKASWRP NLKMLTEHKV TQLTFKGAST TVSGVKAINR KTNKEVTFRA
RKEVILAAGS LHTPQILQLS GIGPKCVVEA AGIKSRVDLP GVGSNLQDHP VAYLNWKVTN
SFPEPNIMTT NETFAAEALA EYQAHRTGPY TKAQSNTIAF LSLPMVTNNT EDMINSLKQQ
VASKYLPGVY SRELIAGYEA QRAILAKQLG EGSVSALEFP FGGSGMVPNS VQKPLSRGTV
HLNPDDPHGE PIVTYNAFTN PFDRAQLASF IAFTRRYFKT NALADMQPQE VSPGEDAQTE
DEIIAKLAAG GPLSLSPSFA HPSSSCPMMP KNKGGCVGAD LRVHGTRKLS IIDASILPII
PSAHLQATMY AVAEKASDII KWRSFWP
//