ID I0K5L7_9BACT Unreviewed; 572 AA.
AC I0K5L7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Gluconate 2-dehydrogenase flavoprotein {ECO:0000313|EMBL:CCG99420.1};
GN ORFNames=FAES_1410 {ECO:0000313|EMBL:CCG99420.1};
OS Fibrella aestuarina BUZ 2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrella.
OX NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCG99420.1, ECO:0000313|Proteomes:UP000011058};
RN [1] {ECO:0000313|EMBL:CCG99420.1, ECO:0000313|Proteomes:UP000011058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUZ 2T {ECO:0000313|Proteomes:UP000011058};
RX PubMed=22689241; DOI=10.1128/JB.00550-12;
RA Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.;
RT "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine
RT Bacterium.";
RL J. Bacteriol. 194:3555-3555(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}.
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DR EMBL; HE796683; CCG99420.1; -; Genomic_DNA.
DR RefSeq; WP_015330519.1; NC_020054.1.
DR AlphaFoldDB; I0K5L7; -.
DR STRING; 1166018.FAES_1410; -.
DR KEGG; fae:FAES_1410; -.
DR PATRIC; fig|1166018.3.peg.3141; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_008878_4_0_10; -.
DR OrthoDB; 1154541at2; -.
DR Proteomes; UP000011058; 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; 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; 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:UP000011058}.
FT DOMAIN 27..328
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 436..559
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 572 AA; 64085 MW; EC21E6487BE8E428 CRC64;
MATFNIDSKK RNTYDAIVIG SGISGGWAAK ELCEKGLKTL VLERGRDVKH IADYPTAMLN
PWELPHRGQV PLEVRNRYSS RSFMREETLH WAIKPDEQPI IEEQPFTWTR GYHVGGKSLL
WARQTQRWSD FDFDGPARDG FAIDWPIRYK DLAPWYSHVE KFAGISGNKD GLDVLPDGEF
LPPFELSCVE QHLKASIDKN YKDRHFIQGR AAHITDPQAI HGEQGRAKCQ HRALCVRGCP
YGGYFSSNAS TLPWAARTGK LTLRPHSVVQ SVIYDEVKKK AVGVRIIDAN SLEPIEYFAN
IIFVNASAIN SNAILLNSQS GRFPNGLGND NGLMGKYLSW HNYRGKANAE FDGLQDKRTD
GKNPSNGYMP RFRNVYKQET TGPASQFLRG YAIGIGGGRG LTSNRDGLGD DLKAQLLNPH
YGNWNISAWM MGECVPIEEN HVRLSTDQTD KYGIPQIILS AKWTDNDARM VQDFNEQITE
MFTLAGFKNV RATDTKSNPG SDIHEMGGVR MGKDPKTSLL NEWNQLHACK NVFVTDGASM
TSTGTQNPSL TYMALTARAV DHAVKELKKR NL
//
