ID A0A1H8NCV5_9RHOB Unreviewed; 805 AA.
AC A0A1H8NCV5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|EMBL:SEO27328.1};
GN ORFNames=SAMN04490248_103112 {ECO:0000313|EMBL:SEO27328.1};
OS Salinihabitans flavidus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salinihabitans.
OX NCBI_TaxID=569882 {ECO:0000313|EMBL:SEO27328.1, ECO:0000313|Proteomes:UP000198893};
RN [1] {ECO:0000313|EMBL:SEO27328.1, ECO:0000313|Proteomes:UP000198893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27842 {ECO:0000313|EMBL:SEO27328.1,
RC ECO:0000313|Proteomes:UP000198893};
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; FODS01000003; SEO27328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8NCV5; -.
DR STRING; 569882.SAMN04490248_103112; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000198893; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000198893}.
FT DOMAIN 6..367
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 371..423
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 427..692
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 718..797
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 805 AA; 88369 MW; AC6436A33E4D757A CRC64;
MKTTTRVVVI GGGVVGCSVL YHLTKLGWPD VMLIERSDLT SGSTWHAAGG FHTLNGDTNM
AALQGYTIKL YKELEEITGL SCGLHHVGGI TLADNRDRFD MLLAERAKHR FMGLETEIVG
PEEIGRIAPV TNVDGILGAL YDPLDGHLDP SGTTHAYARA ARIGGAEIEA HCKVVQTNQR
PDGTWDVVTD KGTVHAEHVV NAAGLWAREV GAMAGVYFPL HPMEHQYLVT EEVPEIAAII
DAGGEHPHVM DPAGESYLRQ EGRGLCIGFY EQPCRPWGID GTPWDFGHEL LPNDFDKIED
SIAFAYRRFP ALERAGIKSV IHGPFTFAPD GNPLVGPVPG MRNYWSAAAV MAGFSQGGGV
GLMLAQWMTQ GETERDTFAM DCARFGDWIT PGYTRPKVIE NYQKRFSVSY PNEELPAARP
FRTTPMYDIF NGMGAVWGHK YGLEVVNYFA AEGEPRLEIP SFRRSNAFDP TAREVAAVRG
AVGINEVHNF GKYRVTGRGA RAWVDRIMAG RVPQLGRVSL SPMLSPRGRL IGDFTISCLS
EEEFQLTASY GAQAFHWRWL RANRDEGVEI ANISDSRTGF QIAGPKAREV LAACTRADIS
DMRFMDVRRL TVGMADCIVQ RLSYTGDLGF EIYCDPMAQR ALWDALWSAG QAHGMRPFGM
RAMMSLRLDK FFGAWLSEFS PDYTAAETGL DRFIAFGKEA NFIGRAAAET ERDAGPARRL
CAFEVAAEDA DVHAYEPIWL DGAVVGFCTS GGYSHHAGKS VAQGFVPADR AQPGLEVEIE
ILGQMRPARL VTEPLFDADG ARMRG
//
