ID   A0A059KJZ6_9BURK        Unreviewed;       583 AA.
AC   A0A059KJZ6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:KDB51700.1};
GN   ORFNames=X805_27270 {ECO:0000313|EMBL:KDB51700.1};
OS   Sphaerotilus natans subsp. natans DSM 6575.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Sphaerotilus.
OX   NCBI_TaxID=1286631 {ECO:0000313|EMBL:KDB51700.1, ECO:0000313|Proteomes:UP000026714};
RN   [1] {ECO:0000313|EMBL:KDB51700.1, ECO:0000313|Proteomes:UP000026714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6575 {ECO:0000313|EMBL:KDB51700.1,
RC   ECO:0000313|Proteomes:UP000026714};
RX   PubMed=24965827; DOI=10.1111/1574-6941.12372;
RA   Park S., Kim D.H., Lee J.H., Hur H.G.;
RT   "Sphaerotilus natans encrusted with nanoball-shaped Fe(III) oxide minerals
RT   formed by nitrate-reducing mixotrophic Fe(II) oxidation.";
RL   FEMS Microbiol. Ecol. 90:68-77(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:KDB51700.1}.
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DR   EMBL; AZRA01000070; KDB51700.1; -; Genomic_DNA.
DR   RefSeq; WP_037482972.1; NZ_AZRA01000070.1.
DR   AlphaFoldDB; A0A059KJZ6; -.
DR   STRING; 34103.SAMN05421778_13130; -.
DR   PATRIC; fig|1286631.3.peg.2670; -.
DR   eggNOG; COG2303; Bacteria.
DR   Proteomes; UP000026714; 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; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968}.
FT   DOMAIN          151..174
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   BINDING         153
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         293
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         519
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   583 AA;  62674 MW;  DEFE6103C6537F7F CRC64;
     MNAPLHPYSS APDHDGLLER LEQALIAGRL DRRGFMRAAM AAGLASAGLP ALADELDTIR
     ANQNERAARL EKSYDYIVIG TGSAGSALVG RLAAARRGAS ILVLEAGGWD SASAVMDPGV
     WFTNLGTERD WGDVAIASPS TNGRAIPEHM GRVVGGGSSI NATIWARPFK ADLDHWAAES
     GDTAWGYEHG LGIYRRMENW QGAPSARYRG QGGPVWCQPA KDPHPVAQAM LAACRSLGLP
     VLDDQNGARE ESAGGFALMN QIIREGRRQS MARAYLYPVL SQPNVTLLVD THVDRLTFAG
     TRTTGVEIRR KGETHRIEAR QEVIVCAGGI NTPKLLMLSG IGPEAQLRQH GIRTLVNAPD
     VGQHFQDHLL HGGCLWEPHE HVPHRNSGAN VAGFVKSQAT LAAPDVNLVQ IELPYASDVV
     GKQFNPPKTS WALCAGLVAP KSRGEIRLRS ADPADRPIVD ARFLSHPDDV KALAHGIELA
     REIGNSPAMK SWVKREVAPA RKLAGQEMAD FVRNGATTYF HQSGTCRMGR DSQAVVDARL
     RVNGVQNLRI ADSSIAPSIP RVATMATCVL IGERMAEILA SAT
//