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Database: UniProt
Entry: F7ZBA8_ROSLO
LinkDB: F7ZBA8_ROSLO
Original site: F7ZBA8_ROSLO 
ID   F7ZBA8_ROSLO            Unreviewed;       819 AA.
AC   F7ZBA8;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|EMBL:AEI94294.1};
DE            EC=1.5.8.4 {ECO:0000313|EMBL:AEI94294.1};
GN   Name=dmgdh1 {ECO:0000313|EMBL:AEI94294.1};
GN   OrderedLocusNames=RLO149_c023240 {ECO:0000313|EMBL:AEI94294.1};
OS   Roseobacter litoralis (strain ATCC 49566 / DSM 6996 / JCM 21268 / NBRC
OS   15278 / OCh 149).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=391595 {ECO:0000313|EMBL:AEI94294.1, ECO:0000313|Proteomes:UP000001353};
RN   [1] {ECO:0000313|EMBL:AEI94294.1, ECO:0000313|Proteomes:UP000001353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149
RC   {ECO:0000313|Proteomes:UP000001353};
RX   PubMed=21693016; DOI=10.1186/1471-2164-12-324;
RA   Kalhoefer D., Thole S., Voget S., Lehmann R., Liesegang H., Wollher A.,
RA   Daniel R., Simon M., Brinkhoff T.;
RT   "Comparative genome analysis and genome-guided physiological analysis of
RT   Roseobacter litoralis.";
RL   BMC Genomics 12:324-324(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; CP002623; AEI94294.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7ZBA8; -.
DR   STRING; 391595.RLO149_c023240; -.
DR   KEGG; rli:RLO149_c023240; -.
DR   eggNOG; COG0404; Bacteria.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_11_1_5; -.
DR   OMA; LGWELHC; -.
DR   Proteomes; UP000001353; Chromosome.
DR   GO; GO:0047865; F:dimethylglycine dehydrogenase activity; IEA:UniProtKB-EC.
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:SF9; FAD DEPENDENT OXIDOREDUCTASE; 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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AEI94294.1}.
FT   DOMAIN          19..376
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          379..432
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          435..705
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          745..811
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   819 AA;  90229 MW;  A9EE7470752E932E CRC64;
     MSLLHAIIGV STMRTHAQAV VIGGGVIGCS ILYHLTKLGW TDVVLLERDE LTSGSTWHAA
     ANIHGLHDNN NITRIQNYTM DLYNALEAET GQSCGVFQPG SLYLAQTEAR EHQLRLQAAK
     AKYYGLHFHE VSRDEAERLH PLVDFDGIRC IMFEPSGGNV DPSGVTNAYA AGTRQNGAEI
     IRFCPVTATE QQPDGTWIVR TTKGDIATEW VVNAAGLWGR EVAALAGLDL PLQPTEHQYF
     VTETIAEIAA LDRRLPSVAD RDGEYYLRQE GKGLLVGAYE KDLRFWAEDG TPQGFGHELF
     ADDLERIEDN MMRAIDRVPA VGEAGIKRVI NGPMIWSPDA NVLFGPAPEL SNYFCCNGII
     PGFSQSGGMG LLAADWIVTG ETRYDMFAWD MARFGTWADK AFTKARVGDQ YANRFKIHFP
     NEERSAGRPL RRRPVYDMQR ERGAVFGLNY GWEHPLYFGY PEGAEDHTEG FTRQDWWHQV
     GAECRMLREN AGVIDISNFA TYRCAGPGAE GWLNSVFANT MPKAVGRSCL TPLIGKRGGI
     AGDFTVTRLG EEEFWVIGSG MAERYHQRFF KAVPLPRDTI FESHTDAMSG FNVAGPRSRD
     MLQRLTNTSL STENFPFMRS KWIELAGVRV LALRVSFTGD LGWELHCATE DQAQLYEALL
     VAGKEVGAGP VGSRALMSLR VEKGYGSWGR EYSPEYWPQE VGLDRLCKMD KAFLNKAAVA
     QTLAKTAREH LVVLALDSGE TDASNADATG GEPIFKDGQG IGRVTSGAYG YSVGMSLALG
     FVSGAQSGDV VEVMVLGRPH QARILAEPPF DPKGLRLRA
//
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