ID A0A0P0SBX8_9PSEU Unreviewed; 498 AA.
AC A0A0P0SBX8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:ALL81792.1};
GN ORFNames=AD017_12445 {ECO:0000313|EMBL:ALL81792.1};
OS Pseudonocardia sp. EC080619-01.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL81792.1, ECO:0000313|Proteomes:UP000066228};
RN [1] {ECO:0000313|EMBL:ALL81792.1, ECO:0000313|Proteomes:UP000066228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL81792.1,
RC ECO:0000313|Proteomes:UP000066228};
RX PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA Van Arnam E.B., Sit C.S.;
RT "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL J. Am. Chem. Soc. 137:14272-14274(2015).
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; CP012184; ALL81792.1; -; Genomic_DNA.
DR RefSeq; WP_060574329.1; NZ_CP012184.1.
DR AlphaFoldDB; A0A0P0SBX8; -.
DR STRING; 1096856.AD017_12445; -.
DR KEGG; pecq:AD017_12445; -.
DR PATRIC; fig|1096856.3.peg.2610; -.
DR Proteomes; UP000066228; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000066228}.
FT DOMAIN 83..106
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 254..268
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 85
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 498 AA; 51759 MW; 32F828EA62ACFD36 CRC64;
MTGGARTDVH DVIVVGAGSA GCTLAGRLAE RGVRTALVEA GEIVVPPEST PIASLAATTP
GHVLNWAYRA TLCQGRECTV PRGRVLGGSG AINGGYFVRA VPADFADWAI PGWSYDDVLP
YYRRLERDLD FCTSDAHGDA GPLRISRPAG HLLAPVTDPF LRACAALGYS EEPDKNAGGR
PGAGPVPTNA VDGKRISAAT AYLPPPWGDA EWQDALTVYG GRAVDTLLFD GDRVTGVRFG
DTELHAAETV VAAGAVGSPA LLQRSGIGPE DTLRSAGVAV RHELPGVGRG WSDHPSVFLP
LRSGLPDPHP DAVAGQAALN LDSGTDPAGD LEVLLFAHPF APGGPAHLMC AVQHPDSRGM
LAITSPEHAD PPRLNFRYLQ TTSDRHRMRA AVRVAAEILR AAGWDRAGPD DGGPAGWELG
NDTRLDEWIH GRLTTSVHLS GSAAMGTGPD AVVGPDLRVH GLDGLRVADT SVLPSAPRRG
PAATAVMIGE RAADLVGG
//
