ID A0A0K1K172_9BURK Unreviewed; 506 AA.
AC A0A0K1K172;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:AKU23102.1};
GN ORFNames=ACZ75_18245 {ECO:0000313|EMBL:AKU23102.1};
OS Massilia sp. NR 4-1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1678028 {ECO:0000313|EMBL:AKU23102.1, ECO:0000313|Proteomes:UP000056897};
RN [1] {ECO:0000313|EMBL:AKU23102.1, ECO:0000313|Proteomes:UP000056897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NR 4-1 {ECO:0000313|EMBL:AKU23102.1,
RC ECO:0000313|Proteomes:UP000056897};
RA Sul W.J.;
RT "Massilia sp. NR 4-1 isolated from rhizosphere of Torreya nucifera in
RT national heritage Bijarim forest, volcanic Jeju Island, Korea.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP012201; AKU23102.1; -; Genomic_DNA.
DR RefSeq; WP_050410153.1; NZ_CP012201.1.
DR AlphaFoldDB; A0A0K1K172; -.
DR STRING; 1678028.ACZ75_18245; -.
DR KEGG; mnr:ACZ75_18245; -.
DR PATRIC; fig|1678028.3.peg.3707; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000056897; 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; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000056897}.
FT DOMAIN 84..107
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT BINDING 86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 94..97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 224
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 506 AA; 54636 MW; F3A90CF6D80CA251 CRC64;
MSDTAFDYII VGGGSAGAVL AARLSEKAGR RVLLLEAGQS FDPHEYPELI YNSNIVAANG
DARYDWGYHA IPGPHDNPVY TPRGKVVGGS SAINAAVACR ATPYCFDLWE KAGVKGWSFE
EVLPYYKKME SSQHGEERWH GRSGPFPIHQ MSRAAISPVQ RAMVDAALEL GYAAVDDFNS
DRNNGAGPNP MNIVNGVRVN TGMAYLTHAV RSRSNLKIQP LCLVDRVRFD GRKAVAVVLA
DGHEIGAREI ILSAGAYGST AILLRSGIGP EAHLAELGIP LLREAAVGTH LRDHPFYWMN
FAGVPELKGQ EKPVVGAQLW TNSSHASSDK ELDIAISPSH LLDGGVSPTG VAFTLGLELM
NAKSVGWVRL ASRDPAQAPI INFNHLDDPD DMRRMVECFR LARKLAATGP LAELTVSEIF
PGAEVENDAE IEQALLKAVS TIQHPCATAR MGRPDDPLAV VDEAARVYGV EGLRVIDASI
FPDIPLINLN PTVIMMAEKL YAEHLA
//
