ID W5WMH6_9PSEU Unreviewed; 482 AA.
AC W5WMH6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=KALB_6019 {ECO:0000313|EMBL:AHH99379.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH99379.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHH99379.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH99379.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(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}.
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DR EMBL; CP007155; AHH99379.1; -; Genomic_DNA.
DR RefSeq; WP_025359294.1; NZ_CP007155.1.
DR AlphaFoldDB; W5WMH6; -.
DR STRING; 1449976.KALB_6019; -.
DR KEGG; kal:KALB_6019; -.
DR PATRIC; fig|1449976.3.peg.6041; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_11; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000019225; 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; 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; 2.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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 Reference proteome {ECO:0000313|Proteomes:UP000019225}.
FT DOMAIN 232..246
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 78
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 198
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 482 AA; 52119 MW; 75D6AD15772E307F CRC64;
MDVIVVGAGS AGCVLTRRLV DSGARVVLLE AGGPDTNPAI HDPARMGELW HGPEDWDHHT
VPQPGAAGRR LHLPRGRVLG GSHSLNAMIW VRGAAQDYDG WQMPGWRWRD VLPVFEQIEK
GPLEIVRNEP LHPVQRSIVD AAVELGVPYN PDYNSGTLDG VSVQQVTMRG GRRLNTWIAY
VLPVLTHPNL TVHTGARVHR LLMSGTRATG VLVELDGHLQ SLHADQVVLA AGALASPAIL
LRSGIGPARE LAALGIEVAA DLPGVGRNLH DHLLSPVIFT TDLREVQPPT PGRSVTQTHL
FWRSRAGLEV PDTQPIHFSV PMYEPWMTGP DTGFSLMAGM ITPHSRGSLR LSGPEVDDEP
LIDLGALTEQ ADLDSLVASV AQCRAIGRSW ALRGEWGARE LYPGPGERDI RSYVRRTAIT
YHHQVGTCRM GLDDQSVVDP RLAVHGITGL RVADASVMPR VISGNTNAPA VLIGEQAAQF
FV
//
