ID A0A1M6R7F3_9RHOB Unreviewed; 835 AA.
AC A0A1M6R7F3;
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:SHK28257.1};
GN ORFNames=SAMN05444000_12433 {ECO:0000313|EMBL:SHK28257.1};
OS Shimia gijangensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1470563 {ECO:0000313|EMBL:SHK28257.1, ECO:0000313|Proteomes:UP000183982};
RN [1] {ECO:0000313|Proteomes:UP000183982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100564 {ECO:0000313|Proteomes:UP000183982};
RA Varghese N., Submissions S.;
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; FQZQ01000024; SHK28257.1; -; Genomic_DNA.
DR RefSeq; WP_073255715.1; NZ_FQZQ01000024.1.
DR AlphaFoldDB; A0A1M6R7F3; -.
DR STRING; 1470563.SAMN05444000_12433; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000183982; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000183982}.
FT DOMAIN 7..381
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 384..438
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 443..722
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 746..825
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 835 AA; 93317 MW; 779028A194E09A0E CRC64;
MKTQVKALVV GGGAVGTSIA YHLAKAGWDD VMLIERDELT SGSTWHAAGL LPLFNMSYAT
THIHKYSVDF YKELEAETGL NAGFAVVGNL RMAQTQDRMD EYMLYASTAE TCGVDYEWLT
PDQIKERWPL IRTDDLKGAI YHTEDGYINP ADVTMAMAKG ARQRGVEIVR KMQADAFHWT
GTHWEVTCTK MIEKGGNLVP SDEQVVITAE HVVTASGNHA QRTAKMLGIK MPAVPVEHTF
IVMDQDPELV KWREAGNPEH PVVRDADAQS YAREERGGWI LGIYEKDAPA RFEHGVPDSF
RADLFPLDLD RIAEQYMAMT ERVPSCADSG LKDDFNGPIC YTPDGNPLVG PAPGLHNMWL
AEGFSFGITA GGGTGYYLAQ MMVDGEAEID MASLDPKRYS QNWMTTEFAA RKNEECYDHV
YVLHHPDEER PAARPLRTAP AFDRQKALGA QFGWVNGWER PNYYGPVDAP DTFDHDARSF
RRGGWWQYAV DEAKAIREGV GLVDATAFTK HVVKGPGATQ FLDWFTCNKL PKVGRINLTY
ALTSHGTTRT EYTIVRNGED NYYLVSAGAW TEYDADYLRK AADEKMAEFG YIEIQDVTTQ
WGVFAIAGPK SRDVLKEIIN DADPETALSN KRFPWLSARQ IELGMCPVNA IRVAYTGELG
WELHHPIEMQ NYLWDLLMSV GEKHDMKLVG ARAQNWLRLE KSYRAFGTEL GRDATPAEAD
LPRFIDNSKE FHGKAEMEAK GIRVKCCTLL IDGPADADPW GREVLYTPEG TRVGRLTSGG
YSVAFKKSIG MGYVTPELAV EGTKLKVKLQ DKLWDAVVTC DSPYDPKNET IRKDG
//
