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Database: UniProt
Entry: C3M979_SINFN
LinkDB: C3M979_SINFN
Original site: C3M979_SINFN 
ID   C3M979_SINFN            Unreviewed;       287 AA.
AC   C3M979;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:ACP26790.1};
GN   OrderedLocusNames=NGR_c30550 {ECO:0000313|EMBL:ACP26790.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP26790.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP26790.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; CP001389; ACP26790.1; -; Genomic_DNA.
DR   RefSeq; YP_002827543.1; NC_012587.1.
DR   AlphaFoldDB; C3M979; -.
DR   STRING; 394.NGR_c30550; -.
DR   KEGG; rhi:NGR_c30550; -.
DR   PATRIC; fig|394.7.peg.5890; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_1_3_5; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000001054; 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; 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   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN          4..241
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   REGION          236..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   287 AA;  32100 MW;  B6619A2FCFFA88B8 CRC64;
     METFDYIVVG AGSAGCVLAN RLSENPAHRV LLLEAGGSDN YHWIHIPVGY LYCINNPRTD
     WCFTTAAEEG LNGRSLFYPR GKVLGGCSSI NGMIYMRGQA RDYDLWRQLG CTGWNWDEVL
     PFFKKSEDHY RGADDMHGAG GEWRVEKARV RWAVLDAFQK AATEAGIPET DDFNRGTNEG
     SGYFDVNQRS GIRWNTAKAF LKPARQRRNL TILTKAHVRK LILEGARVAG VEFQHDGVTK
     RARASRERSP PATPIADHHD RRKGSRDDRR GKPVAAYSAA CVSRIGT
//
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