ID I2GF68_9BACT Unreviewed; 570 AA.
AC I2GF68;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Gluconate 2-dehydrogenase flavoprotein {ECO:0000313|EMBL:CCH52543.1};
GN ORFNames=BN8_01552 {ECO:0000313|EMBL:CCH52543.1};
OS Fibrisoma limi BUZ 3.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrisoma.
OX NCBI_TaxID=1185876 {ECO:0000313|EMBL:CCH52543.1, ECO:0000313|Proteomes:UP000009309};
RN [1] {ECO:0000313|EMBL:CCH52543.1, ECO:0000313|Proteomes:UP000009309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUZ 3T {ECO:0000313|Proteomes:UP000009309};
RX PubMed=22843583; DOI=10.1128/jb.00869-12;
RA Filippini M., Qi W., Jaenicke S., Goesmann A., Smits T.H., Bagheri H.C.;
RT "Genome Sequence of the Filamentous Bacterium Fibrisoma limi BUZ 3T.";
RL J. Bacteriol. 194:4445-4445(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:CCH52543.1}.
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DR EMBL; CAIT01000005; CCH52543.1; -; Genomic_DNA.
DR RefSeq; WP_009281127.1; NZ_CAIT01000005.1.
DR AlphaFoldDB; I2GF68; -.
DR STRING; 1185876.BN8_01552; -.
DR eggNOG; COG2303; Bacteria.
DR OrthoDB; 1154541at2; -.
DR Proteomes; UP000009309; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000009309}.
FT DOMAIN 225..323
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 434..557
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 570 AA; 64215 MW; AF706DA861FE3D3D CRC64;
MANFAIDAKK ENTYDAIVIG SGISGGWAAK ELTGKGLRTL VLERGRDVRH VTDYPTTMLN
PWEFEHRGQL RKEVRDANPI ISKCYAFYEG TEHFFVKDAE HPYVQEKPFD WIRGYQVGGK
SLMWARQTQR WSDFDFDGPA RDGFVVDWPI RYKDIAPWYS YVEKFAGISG NKDGLPQLPD
GEFLPPHEWN CVEKHFQQQM ASKYKDRPVI MGRAAHITKP QPIHLEQGRA QCQHRTICER
GCPYGGYFSS NASTIPWAAR TGKMTLRPDS VVHSIIYDEK LGKATGVRVV DANTKQMQEF
YARIIFVNAA ALNTNLILLN STSSRFPNGL GNDNGLLGKY VAFHNYRAGI SAQYDGYLDS
TTEGKRPNSP YIPRFRNLHK QETDFLRGYA AGFSAGRMSR TNSDGLGASL KENLMNPTLG
GWYVGSHMMG ETIPKETNYV ALDSSLKDPF GIPQLKIAVG YDDNDEKMVK DYLEQMTEMF
TAAGFTNIRT RDDKRNPGLD IHEMGGVRMG KDPKTSLLNK WNQMHNVKNV FVTDGACMTS
TSTQNPSLTY MALSARAVDY AVKQMKAKAI
//
