ID A0A2A5WC79_9GAMM Unreviewed; 563 AA.
AC A0A2A5WC79;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Gluconate 5-dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CNF02_06285 {ECO:0000313|EMBL:PDH33961.1};
OS OM182 bacterium MED-G28.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; OMG group; OM182 clade.
OX NCBI_TaxID=1986256 {ECO:0000313|EMBL:PDH33961.1, ECO:0000313|Proteomes:UP000219329};
RN [1] {ECO:0000313|EMBL:PDH33961.1, ECO:0000313|Proteomes:UP000219329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED-G28 {ECO:0000313|EMBL:PDH33961.1};
RA Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA Rodriguez-Valera F.;
RT "Fine stratification of microbial communities through a metagenomic profile
RT of the photic zone.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:PDH33961.1}.
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DR EMBL; NTJZ01000005; PDH33961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5WC79; -.
DR Proteomes; UP000219329; 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 Pfam; PF13450; NAD_binding_8; 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 208..329
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 427..550
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 563 AA; 61323 MW; D5D7DBE3D0751AC1 CRC64;
MGRITMPQAL NNSVSFDTRE EVDFVVVGSG AAGGILAKEL AAAGHSVVVL EQGPHLQASD
FKHDEWGYEH NNDLVWSTRR GNRQTFRRSE NEEAELQESV LGYAHNVGGS SVHFSGNFWR
FRPIDFMEAS VRGTIAGTNF ADWPITYEDL EPYYTRVDWE IGVSGLQGPW DPPRSRDYPC
PPMPIKGSDV LLERAAKQLG LTPYPAPVAI LSQAHNGRPA CIHCGFCNGY GCEVNAKSSS
MATMIPLALS TGTCELRTMA TVSQISTDEN GRANEVVYFD GEGVEQAQRT KAVVLCANGA
ETPRLLLMSA NNIFPDGLAN SSGFVGQNLM FNGYSSVVGI FDEPVNAWKS LPTTRVVHDY
YELDEHLGFY GGGGIDGRHP SQGTPMEFAL VAPDLFGTAS WGAEFKDSLA YQFSHCAAFD
GHSTSLPLPT NNVTLDPNYQ DTFGRPALRC TYMDHPDDLA TMDWFMKKTI ELMEAAGASN
INGSYPETGQ TGNVHLLGTC RMGSDPMTSV INSDHRAHDV PNLFMCDGSS LVTGGRGQPT
MTIMALAFRA ADRINQLALR NEI
//