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Database: UniProt
Entry: I3V4Z5_PSEPU
LinkDB: I3V4Z5_PSEPU
Original site: I3V4Z5_PSEPU 
ID   I3V4Z5_PSEPU            Unreviewed;       594 AA.
AC   I3V4Z5;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Gluconate 2-dehydrogenase acceptor subunit {ECO:0000313|EMBL:AFK72816.1};
GN   ORFNames=YSA_11149 {ECO:0000313|EMBL:AFK72816.1};
OS   Pseudomonas putida ND6.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=231023 {ECO:0000313|EMBL:AFK72816.1, ECO:0000313|Proteomes:UP000005268};
RN   [1] {ECO:0000313|EMBL:AFK72816.1, ECO:0000313|Proteomes:UP000005268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND6 {ECO:0000313|EMBL:AFK72816.1,
RC   ECO:0000313|Proteomes:UP000005268};
RX   PubMed=22933774; DOI=10.1128/JB.01190-12;
RA   Li S., Zhao H., Li Y., Niu S., Cai B.;
RT   "Complete Genome Sequence of the Naphthalene-Degrading Pseudomonas putida
RT   Strain ND6.";
RL   J. Bacteriol. 194:5154-5155(2012).
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; CP003588; AFK72816.1; -; Genomic_DNA.
DR   RefSeq; WP_004374955.1; NC_017986.1.
DR   AlphaFoldDB; I3V4Z5; -.
DR   KEGG; ppi:YSA_11149; -.
DR   PATRIC; fig|231023.4.peg.5343; -.
DR   HOGENOM; CLU_008878_2_0_6; -.
DR   Proteomes; UP000005268; 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; 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          234..348
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          451..573
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   594 AA;  65244 MW;  E91D1E73F83A4A5C CRC64;
     MATVLNKVDA VIVGFGWAGA IMAKELTEAG LHVVALERGP MQDTYPEGSY PQVIDELTYS
     VRKKLFVDVS KETVTVRHSV NDVALPNRQL GAFLPGKGVG GAGLHWSGVH FRVDPVELRL
     RSHYEERYGR TFIPEGMTIQ DFGVSYEELE PYFDFAEKVF GTSGQAWTVK GQVVGEGKGG
     NPYAPDRSNP FPLPAQKNVV SARLFEKAAT RLGYKPYNLP SANTSGPYTN PYGAQMGPCN
     FCGFCSGYVC YMYSKASPNV NILPALRQVP NFELRPNAHV LRVNLDDRKR KATGVTYIDA
     QGREVEQPAE LVILAAFQFN NVRLMLLSGI GKPYDPVKNE GVVGRNFAYQ NMGTVKAFFD
     KDTYTNNFIG AGGNGIAIDD FNADNFDHGP HGFVGGSPMW VNQAGSRPIA GTSNPPGTPA
     WGSAWKKATA DYYTHQVSMD AHGAHQSYRG NYLDLDPTYR DAYGQPLLRM TFDWQENDIK
     MNQFMVDKLS KIAQAMNPKA IAVLGKQVKD HFNTASYQTT HLNGGAIMGT DPKTSALNRY
     LQSWDVHNVF VPGASAFPQG LGYNPTGLVA ALTYWSARAI REQYLKNPGP LVQA
//
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