ID A0A177CQX3_9PLEO Unreviewed; 485 AA.
AC A0A177CQX3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 19.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:OAG09706.1};
GN ORFNames=CC84DRAFT_1111312 {ECO:0000313|EMBL:OAG09706.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG09706.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG09706.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG09706.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; KV441549; OAG09706.1; -; Genomic_DNA.
DR RefSeq; XP_018040071.1; XM_018175274.1.
DR AlphaFoldDB; A0A177CQX3; -.
DR STRING; 1460663.A0A177CQX3; -.
DR GeneID; 28758760; -.
DR InParanoid; A0A177CQX3; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000077069; 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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT DOMAIN 178..192
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 429
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 472
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
SQ SEQUENCE 485 AA; 52893 MW; 441BED87DB692562 CRC64;
MVFDRGSRAD YNAWEELGNQ GWGWDGLLPY FKKSVDFTAP SVEDAEKFGY TWDESAWGDG
PVQASYPSFQ WQTVRTSWDA WADMEIPLIK EHALGDAVGR FWVPSSEHPV NRTRSYARYA
YYDPIATRPN YHLLVGHKAE SLVLSPKNDA EGVLFYQRDS PGEKKKVKAK KEVILAAGAV
HTPQVLQLSG IGPKAVLEAA NISIKVDAPG VGNNFQDHPQ VYLTCNFTTD VWPNPGTLAN
NATFRAEAQA QYDTNKTGPL TQALNAAFVF LPLNTIHSSP STFHSQLQAQ DPSAYLAPNL
STRVLAGYAA QRRILAKLYN SSDAAVYESP FGGACSRSTL LQKPLSRGHV HINASDPYGE
PAVDFRAYTN PLDIEQGIES LKYTRQYLRN AKFASLTPVE SAPGPAVKDE DTAALEAYVR
LTAGPTSFHA SGTTAMMPQE LGGVVGSDLK VYGVGKVSVV DAGIMPLIPS THLSATVYAM
AEKVR
//
