ID A0A1H3QYT0_9ACTN Unreviewed; 822 AA.
AC A0A1H3QYT0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Dimethylglycine oxidase {ECO:0000313|EMBL:SDZ18510.1};
GN ORFNames=SAMN05660209_04956 {ECO:0000313|EMBL:SDZ18510.1};
OS Geodermatophilus africanus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1137993 {ECO:0000313|EMBL:SDZ18510.1, ECO:0000313|Proteomes:UP000198921};
RN [1] {ECO:0000313|EMBL:SDZ18510.1, ECO:0000313|Proteomes:UP000198921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45422 {ECO:0000313|EMBL:SDZ18510.1,
RC ECO:0000313|Proteomes:UP000198921};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; FNOT01000027; SDZ18510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3QYT0; -.
DR STRING; 1137993.SAMN05660209_04956; -.
DR OrthoDB; 2055370at2; -.
DR Proteomes; UP000198921; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
DR InterPro; IPR028896; GCST/YgfZ/DmdA.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 6..373
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 376..431
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 434..711
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 736..814
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 822 AA; 89249 MW; 039531120E2AFADB CRC64;
MSTTPRVVVI GAGIVGANLA DELTARGWDR VTVVDQGPLP LTGGSTSHAP GLVFQTNASK
TMTAFASYTV EKLKSIDVDG AWCFNQVGGL EVATTPERLA DLHRKQGWAT SWGVESQVVD
VDECVRLHPL VDRDRILGGL HIPSDGLAKA ARAVVALARR AEARGARFQG STRVTGIEQT
GGRVSGVRTP DGVIPADVVV SCAGFWGQEL GAMVGMDVPL LPLAHQFVWT GQVPDLVGRN
DELSEASLPI LRHQDQDLYY RERADRLGIG SYAHRPMPVD LRELPQGDGV RESSMPSMLP
FTEEDFAPAW EQSQLLLPSL RTSKIDNGFN GVFSFTPDGG PLIGESRDVA GFWIAEAVWV
THSAGVGRAV AQLLVDGRSE IDLHGCDVHR FEDVQLAPEY VSETSQQNFV EIYDVLHPLQ
PRLSPRDLRV SPFHTRQQEL GAVFLEGAGW ERPHWYEANA HLLDELPTEW VPPERDAWAG
QFWSPVAAAE AWKTRTAVAM YDMTPLKRLE VSGPGALALL QRLTTGEMDK SVGAVTYTLA
LDEAGGVRSD LTVARLGEQL FQVGANGPLD FDLLLREAPD DGSVQVRDVT GGTCCIGLWG
PRARDLVQRV SADDFTNDGL KYFRAKRARI GGVPVTAMRL SYVGELGWEI YTSADNGQRL
WDVLWRAGQD LGVVAAGRAA FNSLRLEKGY RAWGHDMTTE HDPYEAGLGF AVRRQKEADF
VGRQALAGKG DDTVSRRLSC LTIDDGRSVV LGHEPVFVDG RPAGYVTSAA FGHTVGRPIA
YAWLPASATV GTAVEIEYFG TRIPATVAAE PLVDPGMTRL RG
//
