ID A0A1Y6BX09_9PROT Unreviewed; 815 AA.
AC A0A1Y6BX09;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|EMBL:SMF24347.1};
GN ORFNames=SAMN05428998_10883 {ECO:0000313|EMBL:SMF24347.1};
OS Tistlia consotensis USBA 355.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Fodinicurvataceae; Tistlia.
OX NCBI_TaxID=560819 {ECO:0000313|EMBL:SMF24347.1, ECO:0000313|Proteomes:UP000192917};
RN [1] {ECO:0000313|EMBL:SMF24347.1, ECO:0000313|Proteomes:UP000192917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 355 {ECO:0000313|EMBL:SMF24347.1,
RC ECO:0000313|Proteomes:UP000192917};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; FWZX01000008; SMF24347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6BX09; -.
DR STRING; 560819.SAMN05428998_10883; -.
DR Proteomes; UP000192917; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000192917}.
FT DOMAIN 9..373
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 376..430
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 432..702
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 727..805
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 815 AA; 90066 MW; 49C2E48CBD157D56 CRC64;
MAELPGSARV VIIGGGAVGV SSLYHLARAG WSDAVLLEKN ELTAGSTWHA AGNVPTFSTS
WSVMNMQRYS ASLYRGLGAA VDYPMNYHVT GSIRLAHSDE RMQEFRRVQG MGRYQGMDIE
ILGPDEIRSR YPFIETHDLK GALYDPADGD IDPAQLTQAL AKGARDLGAT ILRFCPATGV
RRDRGEWVVE TAKGEIRCEV VVNAAGYYAR EVGRWFGREV PMMVMSHQYL LTDEIPELAA
WSREVGHKLP LLRDVDSSYY LRQEKTGLNL GPYERNCRAH WATPDDPMPA DFSFQLFDDD
LERLEWYIED AIARVPILGS VGVQRVINGP IPYAPDGNPL IGPMPGVPNA FEACVFTFGI
AQSGGAGKVL AEWVTEGSTE WDMWSCDPRR FTGWCAPDYC VAKGLEVYGH EYAMHFPHHA
WPAGRNRRLS PVHERIAALG GQFGAYNGWE RANWFAAAGD DTSEAATRTW RRDGPWQARV
REECLAVRDA AGILDLPGFS RYRLAGPGVV QWLEGLITGR VPKPGRLGLA YFADARGRVV
TEMSVACLGE EELLLITAAA AEWHDREWLA ARLPADGSIV LEDQTEAWAC QILSGPAARA
ILAAVSDGDL ARPWLSVQEA TLAGRPVRLF RVSFAGELGW EVHSRVEDTP TVFDAIWRAG
EGRGLRPFGM FALNALRLEK GYRAWKGDLS TDYSVLQSGL ERFVAWDKPA FAGRAALMKE
KQEGVARRFV TLLVEAGDCD APYMSTLWHG DQVVGETTSG GWGHRIDRSI ALGMLRADLA
APGQEIEVEI YGERFPATVQ PDRPLWDPEN ARIRA
//
