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Database: UniProt
Entry: A0A223SE47_9ACTN
LinkDB: A0A223SE47_9ACTN
Original site: A0A223SE47_9ACTN 
ID   A0A223SE47_9ACTN        Unreviewed;       527 AA.
AC   A0A223SE47;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Mycofactocin system GMC family oxidoreductase MftG {ECO:0000313|EMBL:ASU86395.1};
GN   Name=mftG {ECO:0000313|EMBL:ASU86395.1};
GN   ORFNames=CDO52_23065 {ECO:0000313|EMBL:ASU86395.1};
OS   Nocardiopsis gilva YIM 90087.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=1235441 {ECO:0000313|EMBL:ASU86395.1, ECO:0000313|Proteomes:UP000215005};
RN   [1] {ECO:0000313|EMBL:ASU86395.1, ECO:0000313|Proteomes:UP000215005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 90087 {ECO:0000313|EMBL:ASU86395.1,
RC   ECO:0000313|Proteomes:UP000215005};
RA   Yin M., Tang S.;
RT   "The complete genome sequence of Nocardiopsis gilva YIM 90087.";
RL   Submitted (AUG-2017) 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}.
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DR   EMBL; CP022753; ASU86395.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A223SE47; -.
DR   KEGG; ngv:CDO52_23065; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000215005; 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; 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; 1.
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:UP000215005}.
FT   DOMAIN          13..307
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          386..516
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   BINDING         95
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         103..106
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         232
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   527 AA;  53829 MW;  898FC2D3EFAC4BE0 CRC64;
     MPGVRAVLGA DVVIVGAGPT GSALAVRLSD DTTPGAARSV QLLEAGPAPA TCDAVPPEVL
     DGTRMAAARP GHALNWSFTG KVAPGTRRPV PRGRVAGGSG AINGGVFIRG TREDFDAIAA
     LGHPDWSYER VLPSFAAVEH DHDFAGPPHG RRGPVPVRRT FPGSASPLTE AFWAACRGLG
     YPWEPDKNAP GPPGVGPVPV NVVSGIRHSA LLTHLLPHAG RPHLTVRGGV LVRRILFAGT
     RAIGVEAETE GRVQVVRGDE IVLAAGAIGS ARLLLLSGVG PADELADLGI RVVHGAPAVG
     RAVTDHPGVA VGITPVPSAV PAARTAVVEA ALHAVSTAAD EGTGARRDGD LEIMPYTAPF
     TELIPGGAGT PPGEVAFGVT LLRTASSGAI RLASADPHAP PLITYRHLTS AADRARLREG
     VRRCAEILTS APLRRLTASY GGPPAAVLGS DRALDTWIGE RVSTANHLSG GCAMGEVTDA
     QGRVHGVTGL RVADSSILPR APSRGTAATA AMMGEHLARS FPPTLES
//
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