ID A0A1W0BC34_9NOCA Unreviewed; 492 AA.
AC A0A1W0BC34;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Mycofactocin system GMC family oxidoreductase MftG {ECO:0000313|EMBL:ONM47094.1};
GN ORFNames=B0T46_19105 {ECO:0000313|EMBL:ONM47094.1};
OS Nocardia donostiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1538463 {ECO:0000313|EMBL:ONM47094.1, ECO:0000313|Proteomes:UP000188836};
RN [1] {ECO:0000313|EMBL:ONM47094.1, ECO:0000313|Proteomes:UP000188836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X1655 {ECO:0000313|EMBL:ONM47094.1,
RC ECO:0000313|Proteomes:UP000188836};
RX PubMed=26914251; DOI=10.1007/s10482-016-0667-8;
RA Ercibengoa M., Bell M., Marimon J.M., Humrighouse B., Klenk H.P.,
RA Potter G., Perez-Trallero E.;
RT "Nocardia donostiensis sp. nov., isolated from human respiratory
RT specimens.";
RL Antonie Van Leeuwenhoek 109:653-660(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}.
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:ONM47094.1}.
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DR EMBL; MUMY01000017; ONM47094.1; -; Genomic_DNA.
DR RefSeq; WP_077119320.1; NZ_MUMY01000017.1.
DR AlphaFoldDB; A0A1W0BC34; -.
DR STRING; 1538463.B0T36_11390; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000188836; 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; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023978; GMC_oxidoreductase_bact.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR NCBIfam; TIGR03970; Rv0697; 1.
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.
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:UP000188836}.
FT DOMAIN 2..301
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 351..486
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT BINDING 82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 227
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 475..476
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 492 AA; 51989 MW; 8A8300B003BCD319 CRC64;
MVDTLVIGAG TAGCVVAARA SADPRHTVRV VEAGPVWASA AQFPPQLRDA TRLPLDDAAP
WLWRYPVALT EERPGSIVRG RVAGGSGTIN GCYFVRPPAA DFTAWSQVAP GWSTDEVLPH
FRELEHDYDY GDQPGHGNAG PVPVRRTTTP APLTEQFLQA CTAAGFTELA DLNALPADSA
ASGAGLVPCN VGPVAGDGFR ARVATAQSYL LPALSRPNLT VTGGTTVSTI RFRGGRAIGA
DCVRDGVPET VWADRVVVCA GAIESAALLL RSGIGPPEQL RALGIPVVQA APVGRWCTDH
PEIGIEYRHR AQLDRTVALE SVLELGDIEI RPYTVAFAPD TRHLGIALMR PHASGTLRLR
SADPLASPII EYRYLANAVD RTRLHEAAEV AGRLLDRMGA EPVGDIPDRD AAGAEHADGW
LLRLLGTSQH LSGTCRMGVS GDPRAVVDER CRVHGVPGLS VADLSIVPVP LGRGPQATTV
MLAERAATFL RG
//