ID A0A1M7D3P7_9RHOB Unreviewed; 811 AA.
AC A0A1M7D3P7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|EMBL:SHL74075.1};
GN ORFNames=SAMN05444414_1342 {ECO:0000313|EMBL:SHL74075.1};
OS Roseovarius marisflavi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1054996 {ECO:0000313|EMBL:SHL74075.1, ECO:0000313|Proteomes:UP000184191};
RN [1] {ECO:0000313|EMBL:SHL74075.1, ECO:0000313|Proteomes:UP000184191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29327 {ECO:0000313|EMBL:SHL74075.1,
RC ECO:0000313|Proteomes:UP000184191};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRBN01000034; SHL74075.1; -; Genomic_DNA.
DR RefSeq; WP_073200520.1; NZ_FRBN01000034.1.
DR AlphaFoldDB; A0A1M7D3P7; -.
DR STRING; 1054996.SAMN05444414_1342; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000184191; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
FT DOMAIN 6..364
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 368..421
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 428..699
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 724..803
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 811 AA; 89302 MW; 53C29F3549167A1C CRC64;
MKSRTKVVVI GGGIAGCSTL YHLTQEGWSD VVLIERDELT SGTTWHSAAQ VTNFGMNQTM
VGLKSHSIQL YKKLRDDPDY PVGYHNGDGG IRLANTEAQM QGYRHFASMA RGMGVEFEII
DAEECARRHP LISTDNLLGG LWDGEDGDID PAQLCQALVF HARKAGAKVY RQTEVIGLTQ
HSDDTWTVET EKGNIDADIV VNACGYRVNE VGGMMGVHHP VVSMEHQYFV TEDIPAIVEA
GHRMPLLRCP ISDYYCRQEK NGLLVGFYEQ DCTTWGMDGI SPSFSNALCP DDLDRVMDVL
EGAFERMPVL TEVGIKRVVN GPITYTIDGA PLVGPIPGKR NAFCIIGLRA GIGEGGGHGW
LLAQQIVHGE ACYDTWCIDP RRFAGHTNVE LTALKAVEDY QNEFRFHFPH EHRPAGRPGK
TTPLTPILAA QGAEFTVVNG WERVDYIKPT PDFHPTLSFH FDEAFDVIAA EVKTLQENVG
LAEVNGFNRI EITGADRHAF LDRMFCGTVT RRDGRVGLGY LLNRHGMVKG EATVANLPAS
DRGPARVWYG SAAASETHDM DWLKTHVQDA EYVQLRPLTN DQTILVLAGP KARDVMQAVS
RADWSKEGFP WLSVRECFIG FAPATVMGVS FSGELAYEIH VPNASLYAAY LALREAGEPH
GLRLFGARAI DSMRMEKGYL QWKADLLTEF TPFETSLGRF VKLDKGDFIG KDALLARHES
GLRKKLVTLR LDAPHAPAHG GASVIKDGEV VGTVTSGDWG HRVGMNLAYA FVDTDVMEVG
TAMELDLCGE MVPVQVIDPS PYDPANTRLR E
//