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Database: UniProt
Entry: I0QVJ2_9GAMM
LinkDB: I0QVJ2_9GAMM
Original site: I0QVJ2_9GAMM 
ID   I0QVJ2_9GAMM            Unreviewed;       529 AA.
AC   I0QVJ2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:EIC85315.1};
GN   ORFNames=SPM24T3_07749 {ECO:0000313|EMBL:EIC85315.1};
OS   Serratia sp. M24T3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=932213 {ECO:0000313|EMBL:EIC85315.1, ECO:0000313|Proteomes:UP000011072};
RN   [1] {ECO:0000313|EMBL:EIC85315.1, ECO:0000313|Proteomes:UP000011072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M24T3 {ECO:0000313|EMBL:EIC85315.1,
RC   ECO:0000313|Proteomes:UP000011072};
RX   PubMed=22740681; DOI=10.1128/JB.00670-12;
RA   Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT   "Draft Genome Sequence of Serratia sp. Strain M24T3, Isolated from Pinewood
RT   Disease Nematode Bursaphelenchus xylophilus.";
RL   J. Bacteriol. 194:3764-3764(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIC85315.1}.
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DR   EMBL; AJHJ01000006; EIC85315.1; -; Genomic_DNA.
DR   RefSeq; WP_009636149.1; NZ_AJHJ01000006.1.
DR   AlphaFoldDB; I0QVJ2; -.
DR   STRING; 932213.SPM24T3_07749; -.
DR   PATRIC; fig|932213.3.peg.1561; -.
DR   eggNOG; COG2303; Bacteria.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000011072; 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   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          221..313
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          401..521
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          146..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  58430 MW;  E94B418445A04DB8 CRC64;
     MTKQYDADVI VIGSGALGSN AAHTLALKGR SVIILEAGER IPRWKIVENF RNSSKKANYN
     SPYPNQPWAH HSYDEQYIEN TGSFDFRPGM LKLVGGTTWH WAAACWRYLP NDMKLKTLYG
     VGRDWPMEYS ELEPFYQRAE EALGVCGSDT DDQSGQAGQP FPPRSKPYPM EPEGETYLFQ
     RVKSRISPAG YHFIHEPNGR ATRPYDGRPA CSGNNNCMPV CPIGSMYSGD KHAQHAEDAG
     AKLLTDSTAW KLEKGPDGKI VAVHVRSSTG EDTRLTAKYF IVAAHGLETA KLLLISDVAN
     SSDQVGRNLM DHTGMGLQFL ADEPVWPGRG AVQQGGIFNY RDGDFRKKHS AIKHAMSNNV
     PNMTVAQRLI AKGVMGSELD KQIRHQAARW VDISTVFEIL PHATNTVRPS TTRKDALGIP
     MLTVHYEVDD YVKAAKGVVD ADYKKFVSLM GGTVIEDNTG WQNRDHLMGT VIMGDNQKDS
     VVNHECRTWD HSNLFLATTG VIPASGVINP TLTGVALSIR AAEIIDKEI
//
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