ID A0A0W7YZH5_9BURK Unreviewed; 540 AA.
AC A0A0W7YZH5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:KUF40567.1};
GN ORFNames=AS359_03355 {ECO:0000313|EMBL:KUF40567.1};
OS Comamonas kerstersii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=225992 {ECO:0000313|EMBL:KUF40567.1, ECO:0000313|Proteomes:UP000053300};
RN [1] {ECO:0000313|EMBL:KUF40567.1, ECO:0000313|Proteomes:UP000053300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12322-1 {ECO:0000313|EMBL:KUF40567.1,
RC ECO:0000313|Proteomes:UP000053300};
RA Ming D., Wang M., Hu S., Zhou Y., Jiang T.;
RT "Complete genome sequence of a multi-drug resistant strain Acidovorax sp.
RT 12322-1.";
RL Submitted (DEC-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}.
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:KUF40567.1}.
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DR EMBL; LPXH01000027; KUF40567.1; -; Genomic_DNA.
DR RefSeq; WP_058879993.1; NZ_LPXH01000027.1.
DR AlphaFoldDB; A0A0W7YZH5; -.
DR STRING; 225992.B5M06_07375; -.
DR Proteomes; UP000053300; 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 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; 1.
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; PS00624; GMC_OXRED_2; 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:UP000053300}.
FT DOMAIN 82..105
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 258..272
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 219
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 540 AA; 57845 MW; 1222A9093F8B2AE1 CRC64;
MGEAFDYIVI GAGSSGSVLA GRLSESGLHQ VCVLEAGGAD DSALLQCPGG LAGLAKTGHF
NWSMATVPQP GLGGRVGYQP RGKGLGGSSS INAMIYLRGQ PEDFDWWAAQ GNPGWAWEDV
KPWFLKAEHQ ERGADAFHAQ GGPLNVADLQ QPNPLSQDFV AAGVQAGFPA NTDFNAASQE
GVGLYQVTQK SGERCSAAKA YLTPHLHRRN LHVRMGAQVL RIVLEHSDQG LRATGVEYVR
GGVRHSVHAR REVLLSAGAL LSPQVLMLSG IGPAAHLQEV GIAPVHDLPG VGSHLHDHLD
ATLVLDAPQL TQSFGLSLSG GWHLAQGAWE WWRHRTGILT SNFAEAGAFL RSSPEEALPD
LQLHFVVAKL LDHGRKTVRG HGYSCHVCVL RPRSRGTVRL RSADPLTLPA VDPNFLADAD
DLQRTVRGVQ IVRRILAQPA LARHGARELP ASAAAQTSEQ IADWVRQYAD TIYHPVGTCR
MGPGPQDVVD HQLRVHGVQG LRVVDASIFP CITSGNTNAP CIMLGEKAAH MVLAEAQRWA
//
