ID A0A1P9WZ10_9BACT Unreviewed; 571 AA.
AC A0A1P9WZ10;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:AQG80617.1};
GN ORFNames=AWR27_15570 {ECO:0000313|EMBL:AQG80617.1};
OS Spirosoma montaniterrae.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1178516 {ECO:0000313|EMBL:AQG80617.1, ECO:0000313|Proteomes:UP000187941};
RN [1] {ECO:0000313|EMBL:AQG80617.1, ECO:0000313|Proteomes:UP000187941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY10 {ECO:0000313|EMBL:AQG80617.1,
RC ECO:0000313|Proteomes:UP000187941};
RA Oliw E.H.;
RL Submitted (JAN-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; CP014263; AQG80617.1; -; Genomic_DNA.
DR RefSeq; WP_077132045.1; NZ_CP014263.1.
DR AlphaFoldDB; A0A1P9WZ10; -.
DR STRING; 1178516.AWR27_15570; -.
DR KEGG; smon:AWR27_15570; -.
DR OrthoDB; 9787779at2; -.
DR Proteomes; UP000187941; Chromosome.
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 InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 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 Reference proteome {ECO:0000313|Proteomes:UP000187941}.
FT DOMAIN 19..67
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 111..345
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 436..558
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 571 AA; 63591 MW; DF666B63A738052A CRC64;
MNRNIRATSN HTAPADRYDA IVVGSGISGG WAAKELTQKG LRVLLLERGR PVEHVTDYST
AMQAPWEFPH RGRKTFDDTE AYRIQSKNYG VDETNKHFYV NEIENPYVQT QPNEFVWARG
HQVGGRSLTW GRQCYRWSDL DFEANLKETI GVDWPIRYAD IAPWYTYVEK FVGISGSREG
MAHLPDSEFL PPMPMNCAEK HLSATVAKTY ADRRVIIGRV ANLTQPKIAR GVCQFRNLCD
RGCPFGGYFS SNAATLPVAA ATGRLTLRPH SIVTEVLYDD RTKRAKGVAV LDAETGKTYE
YFSRILFLNA STISTAFLML RSTSARFPNG LGNDSGELGR NLMTHSKINV RGHYEGFLDQ
YTFGRRANGI YVPRFRNVAK AHPDFRRGYN YQGGASRPRT SPADVQAGFG ADLKEALTKP
APYWNVGLTG FGEQLPDPAN VVRVSQTVKD KWGLPVPELT WRWLPNDIAM MTDAAREATA
MLDAAGCRNI VAEPISQLRS TVHEMGTARM GRDPKTSVLN AHNQIHACKN VFVTDGACMT
SASCVNPSLT YMALTARAAD FAVKELKRQN L
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