ID I0QQE3_9GAMM Unreviewed; 595 AA.
AC I0QQE3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Gluconate 2-dehydrogenase {ECO:0000313|EMBL:EIC83516.1};
GN ORFNames=SPM24T3_16723 {ECO:0000313|EMBL:EIC83516.1};
OS Serratia sp. M24T3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=932213 {ECO:0000313|EMBL:EIC83516.1, ECO:0000313|Proteomes:UP000011072};
RN [1] {ECO:0000313|EMBL:EIC83516.1, ECO:0000313|Proteomes:UP000011072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M24T3 {ECO:0000313|EMBL:EIC83516.1,
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 -!- 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:EIC83516.1}.
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DR EMBL; AJHJ01000023; EIC83516.1; -; Genomic_DNA.
DR RefSeq; WP_009637954.1; NZ_AJHJ01000023.1.
DR AlphaFoldDB; I0QQE3; -.
DR STRING; 932213.SPM24T3_16723; -.
DR PATRIC; fig|932213.3.peg.3361; -.
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; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 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;
FT DOMAIN 236..349
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 451..574
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 595 AA; 65442 MW; D22623133AC02823 CRC64;
MSKTMQKVDA VIVGFGWAGS IMAKELTEAG LSVVALERGP SRDTYPDGAY PQVVDELTYN
IRKKLFQDLS KSTVTIRHNM TQTAMPYRQL NAFLPGTGTG GAGLHWSGVH FRVDPAELNL
RSHYEQRYGK KFIPEGMTIQ DFGVNYNELE PFFDKAEKVF GTSGSPWTIK GQQQPGAQGT
GNPFAPDRSD KFPLPAQKRT YSAQLFAQAA EAVGYHPYDL PSANTSGPYT NTYGAQMGPC
NFCGYCSGYA CYMYSKASPN VNILPSLRQE SQFELRNNSY VLRVNLTDDK KRATGVTYVD
ALGQQVEQPA DLVILSAFQF HNVHLMLLSG IGKPYDPVTN EGVVGRNFAY QNLTTIKAFF
ETDKFTNTFI GAGGNGVAVD DFNADNFDHG KYGFVGGSPF WVNQAGSKPI SGVATPPGTP
NWGSKWKAAV ADSYTHNVSM DAHGAHQSYR ANYLDLDPTY KDIYGQPLLR MTFDWQPNDI
KMSQFMHDKM HKIAVAMNPK LISGSPKTAD THFDSTVYQT THMNGGAIMG EDPKTSAINR
YLQSWDVHNV FVPGASAFPQ GLGYNPTGMV AALTYWSAKA IRETYLKNPG PLVQA
//
