ID A0A0F2S1X4_9RHOB Unreviewed; 814 AA.
AC A0A0F2S1X4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|EMBL:KJS43432.1};
GN ORFNames=VR71_10250 {ECO:0000313|EMBL:KJS43432.1};
OS Roseovarius sp. BRH_c41.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1629709 {ECO:0000313|EMBL:KJS43432.1, ECO:0000313|Proteomes:UP000033676};
RN [1] {ECO:0000313|EMBL:KJS43432.1, ECO:0000313|Proteomes:UP000033676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c41 {ECO:0000313|EMBL:KJS43432.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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:KJS43432.1}.
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DR EMBL; LADY01000032; KJS43432.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2S1X4; -.
DR PATRIC; fig|1629709.5.peg.4390; -.
DR Proteomes; UP000033676; 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;
FT DOMAIN 9..377
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 380..428
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 436..700
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 726..800
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 814 AA; 90428 MW; 82C8A703840093E1 CRC64;
MAEFPGTARV VIIGGGVVGA SCLYHLAKAG WADCVLLEKN ELTAGSTWHA AGNVPTFSTS
WSVMNMQRYS TELYARLGAE VEYPMNYHQT GSIRLAHSRE RMQEFQRARG MGKVQGMDLD
ILGVDEIKAR YPFLETHDLQ GALYDPNDGD IDPAQVTQAL AKGARDMGAQ ILRFTPATGV
RRENGEWIVA TEKGEIRCEY VVNAAGYYAQ RVGEWFKPYG GRTVPMMVMS HQYLLTDEIP
ELEAWSREAG HKLPLLRDVD SSYYLRQEKY GLNLGPYERN CKAHWVKPDD PMPEDFSFQL
YPDDLERLEW YIEDAMARVP LLGQAGISKV INGPIPYAPD GLPLIGPMPG VPNAFEACVF
TFGIAQGGGA GKVLAEWVTE GATEWDMWAC DPRRFTDYTD AEYCVAKGME VYGHEYAMHF
PWHRWPAAPD RKVSPVHERV KALGGVMGVY NGWERANWFA KPGDDTSEAA TQTWDRAGPW
EARIREECEA VRDACGVLDL PGFTRLWIEG TGADDWLRGF VTGGLPKVGR MNLVYVADKR
GRIVTEFSCI RLKEDSFVLI TAATAQWHDG ELVRRALPEG LSLRETTTER DALLLAGPKS
RDILAGLTDA DLSLPWLSHQ HATVAGQKAF LARVSFTGEL GWEIHAENAA IPTIYEALMA
AGVKPFGMFA LNSLRIEKGY RAWKGDLSTD YSMLEGGLER FVKFDKPQDF AGKAALLAEK
QRGVKKRFVT LIVEAKAADA PYMSTLWHEG QIVGETTSGA WGYRVGASVA LGMLRADLAV
PGTEIEVEIY GERCRAVVQP DAPLWDAENE RLRA
//