ID A0A1X7NIS3_9RHOB Unreviewed; 832 AA.
AC A0A1X7NIS3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|EMBL:SMH37316.1};
GN ORFNames=SAMN05661107_0786 {ECO:0000313|EMBL:SMH37316.1};
OS Maritimibacter sp. HL-12.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=1162418 {ECO:0000313|EMBL:SMH37316.1, ECO:0000313|Proteomes:UP000193836};
RN [1] {ECO:0000313|EMBL:SMH37316.1, ECO:0000313|Proteomes:UP000193836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-12 {ECO:0000313|EMBL:SMH37316.1,
RC ECO:0000313|Proteomes:UP000193836};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; FXBQ01000001; SMH37316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7NIS3; -.
DR STRING; 1162418.SAMN05661107_0786; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000193836; 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; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR13847:SF187; DIMETHYLGLYCINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000193836}.
FT DOMAIN 7..380
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 383..436
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 440..721
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 745..818
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 832 AA; 92676 MW; 32AC94F5E4D25B50 CRC64;
MKTHVKALVV GGGAVGASIA YHLARAGWTD VMLLERDELT SGSTWHAAGL LPLFNMGYAT
THIHDYSVKF YKALEEETGL NAGFSVVGNL RMAQSAERMD EFQLYASTAE TVGIPYEFLT
PDEIKARWPL VRTDDLRGAL YHPTDGYINP ADVTMAMAKG ARQRGVVIER KWQVDGYRWT
GSEWIVTVTK MGEKGGNLVP TEEQVEIHAE HVVTATGNHA QRTARLLGIK IPAIPVEHQF
IVTEPDPALL EYRKTHGEHP VLRDADAKWY VREERGGWIL GPYERNAPAR FEYGVPDSFR
ADLFPLDLDR IEEEYMSMIH RIPSSEEVGL KDDFNGPICY TPDGNPLVGP APGLRNMWLA
EGFSFGITAA GGTGYYLAQM MVEGEAEIDM ASLDPKRYGD WMTTEYAARK NEECYEHVYI
LHHPDEERPA CRPLRTAPAY DRQKALGAQF GQVNGWERPN YYGPLDASED FDHEARSFRR
GGWWQYARAE AEAIREGAGL IDATAFTKHL VRGPGATAFL DWFTTNKLPN VGRINLTYAL
TETGTTRTEY TIVRYAEDEY VLISSGALTA YDGDYLRKAA ADRIGDLGYI EVHDITTQYG
VFAIAGPKSR DVLKELVKDA DPDTVLGNKR FPWLSMRNIE LGMCPVHAVR VAYTGELGWE
LHHPIEMQNY LWDQLMAAGA KHGLKLVGAR AQNWLRQEKS YRAFGTELGR DATPLEAGLD
RFVDLSKDFL GKTAMEATGI RAMCVTLLID GPDDADPWGR EALYAGDTKV GRLTSGGYSV
VFGKSIGMGY VRPDLAAPGT KLQVMMQGRL WDAEVAEDSP HDPQNARIRL DG
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