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
//