ID V9W0J7_9RHOB Unreviewed; 523 AA.
AC V9W0J7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN ORFNames=METH_22830 {ECO:0000313|EMBL:AHD03668.1};
OS Leisingera methylohalidivorans DSM 14336.
OG Plasmid unnamed {ECO:0000313|EMBL:AHD03668.1}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=999552 {ECO:0000313|EMBL:AHD03668.1, ECO:0000313|Proteomes:UP000018780};
RN [1] {ECO:0000313|EMBL:AHD03668.1, ECO:0000313|Proteomes:UP000018780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14336 {ECO:0000313|EMBL:AHD03668.1,
RC ECO:0000313|Proteomes:UP000018780};
RC PLASMID=2 {ECO:0000313|Proteomes:UP000018780};
RG DOE Joint Genome Institute;
RA Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (SEP-2013) 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; CP006775; AHD03668.1; -; Genomic_DNA.
DR RefSeq; WP_024092465.1; NC_023136.1.
DR AlphaFoldDB; V9W0J7; -.
DR KEGG; lmd:METH_22830; -.
DR PATRIC; fig|999552.6.peg.4509; -.
DR HOGENOM; CLU_002865_7_2_5; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000018780; Plasmid 2.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}; Plasmid {ECO:0000313|EMBL:AHD03668.1}.
FT DOMAIN 80..103
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 251..265
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 459..460
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 523 AA; 57054 MW; 3F6E13D28513FB58 CRC64;
MDRFDFIICG AGTAGCILAN RLSADPEIKV LLLEAGQVMK APKLDAYGAS VDHWDSPLDW
AFRSEPQRHL NNRRILLNRG KGLGGSSGIN WGMYVRGNRG DFDHWAQLGN RGWSYDEILP
SMIKSEASRV IEDGYHGTSG EISVELPRNR HPLQEMCFEA YEDLGVPRNP DYNGANQEGC
FYYQFTTNHG RRVSAADAFL NPIEDRPNLT VVTGAHLSGV MFVGTRATGV TFVKGRDSQA
VSAGEVILSM GAIGSPHLLM LSGIGPANHL SEHDIPCRHD LAGVGQNLLD HLGGPRIGFT
LREPEKFGFP IAGEAASLKE FNATGTGPLA TTGVDAGAFV RLRDSDEYPS AQSICNVSNT
HLDRRIDMPP RLSFGGYICR TVSKGTVRLA SASPFDRPLV DPNYLSDPMD LETHVAFLKF
QRRMIEHPIF APVRGEVYGP KMDRENIIKA TREGASTTWH QTSTCRMGVD PLAVVGPDLT
VRGLENLRVI DASVFPTMTS GNTNAPTMMV AEKGAALILQ KSF
//
