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Entry: A0A1X6ZSH9_9RHOB
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Original site: A0A1X6ZSH9_9RHOB 
ID   A0A1X6ZSH9_9RHOB        Unreviewed;       529 AA.
AC   A0A1X6ZSH9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Alcohol dehydrogenase [acceptor] {ECO:0000313|EMBL:SLN59494.1};
DE            EC=1.1.99.- {ECO:0000313|EMBL:SLN59494.1};
GN   Name=alkJ {ECO:0000313|EMBL:SLN59494.1};
GN   ORFNames=ROA7450_03079 {ECO:0000313|EMBL:SLN59494.1};
OS   Roseovarius albus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1247867 {ECO:0000313|EMBL:SLN59494.1, ECO:0000313|Proteomes:UP000193061};
RN   [1] {ECO:0000313|EMBL:SLN59494.1, ECO:0000313|Proteomes:UP000193061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7450 {ECO:0000313|EMBL:SLN59494.1,
RC   ECO:0000313|Proteomes:UP000193061};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; FWFX01000010; SLN59494.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X6ZSH9; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000193061; 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:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 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; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Oxidoreductase {ECO:0000313|EMBL:SLN59494.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193061}.
FT   DOMAIN          80..103
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          253..267
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         82
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         217
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   529 AA;  57906 MW;  1BBCD5B0F493F061 CRC64;
     MEADFIIIGA GSAGCVLANR LSKNPNNRVV LLEAGGKDTN PWIHIPVGYF KTIHNPTVDW
     CYETEPDPGL NGRSIEWPRG KVLGGSSSLN GLLYVRGQPQ DYDRWRQMGN EGWAWDDVLP
     LFKRSEKNER GADEYHGDQG GLSVSNMRIQ RPITDAWVAA AQAAGYKFNP DYNGADQEGV
     GFFQLTSRNG RRCSSAVAFL NPAKSRENLQ IITNAHVQRI DIEDKCATGV TFKDRSGTLQ
     TIKANREVIL SAGAINSPQI LMLSGIGEAA QLNEHGIDII ADLPGVGKNL QDHLQARLVY
     KCNEPTLNDE VSSLFGQAKI GLKYLMFRAG PMTMAASLAT GFMKTRDELE TPDIQFHVQP
     LSAENPGKGA DKFSAFTMSV CQLRPESRGE IRLTSADPKV YPKIIPKYLS TETDCRTIVE
     GINIARRIAR HAPISSKISE EFRPNANLDI EDYEATLDWA RSNTASIYHP TGTCKMGSGA
     DAVVDHHLKV HGIKGLRVAD CSIMPEIVSG NTNAPAIMIG EKASDLVLK
//
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