ID A0A1Q9S2R8_9PSEU Unreviewed; 606 AA.
AC A0A1Q9S2R8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN ORFNames=BJF90_24830 {ECO:0000313|EMBL:OLT03942.1};
OS Pseudonocardia sp. CNS-004.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1904967 {ECO:0000313|EMBL:OLT03942.1, ECO:0000313|Proteomes:UP000186863};
RN [1] {ECO:0000313|EMBL:OLT03942.1, ECO:0000313|Proteomes:UP000186863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNS-004 {ECO:0000313|EMBL:OLT03942.1,
RC ECO:0000313|Proteomes:UP000186863};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
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:OLT03942.1}.
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DR EMBL; MKJV01000078; OLT03942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9S2R8; -.
DR Proteomes; UP000186863; 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; 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.
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:UP000186863}.
FT DOMAIN 108..131
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 281..295
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 242..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 606 AA; 65337 MW; 72644F498444EB5D CRC64;
MRTGAGEDVR PCAGEGEEDV RGEVSATGCD VLIVGGGPAG CILANRLSAD PSVRVLVLEA
GGPDHWWDLR IQLPLAMGFP VGHRSFDWRY ESEPEPGLGS RKLHHPRGKV LGGSSSINGM
LYERGHRASY DRWADEAESP EWDYAHCEPY FRRLEGCVGE PRGTGRGRSG PQALQRGPAD
GPIFDAFFEA AQQAGYKVVP DATTTRRRAS PRWIRRCGAA SVPRPRSRTC TRWRTGRTWR
SAATPRSARS CSRARVRGGP VPGQERGDAH VRASETILSA GAIATPQILQ LSGVGDGEHL
RGLGIPVVHH LPGVGERLQE HLAVHIQHRC IQPVSMSDIR NKAKWPGVVL DALVFGKGPG
TRNPMQAGGF VRSDVAEGSE PDLMYLLAPL AMNSSDESVE VSAHGYQMHV GVMRSESRGS
VKIASPVPAV HPKIVANFLS DPKDRDRWIN AVERGRHLLG QPAFRHLDGG ETLPGPGVRT
GEEIMAWVRR TGRVGYHPSC TAAMGRGEMA VVDPDTMRVH GLDGLRVVDA SVMPSLTNAN
TLAPTMMIAE KSADIMLGNA PLPPNRPERP RLVPAPEKPV VVSDVQRPAS ALPSGAALFA
ETKQTT
//
