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Database: UniProt
Entry: Q98KX1_RHILO
LinkDB: Q98KX1_RHILO
Original site: Q98KX1_RHILO 
ID   Q98KX1_RHILO            Unreviewed;       817 AA.
AC   Q98KX1;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|EMBL:BAB48692.1};
GN   OrderedLocusNames=mlr1280 {ECO:0000313|EMBL:BAB48692.1};
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB48692.1, ECO:0000313|Proteomes:UP000000552};
RN   [1] {ECO:0000313|EMBL:BAB48692.1, ECO:0000313|Proteomes:UP000000552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC   {ECO:0000313|Proteomes:UP000000552};
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; BA000012; BAB48692.1; -; Genomic_DNA.
DR   RefSeq; WP_010910046.1; NC_002678.2.
DR   AlphaFoldDB; Q98KX1; -.
DR   KEGG; mlo:mlr1280; -.
DR   PATRIC; fig|266835.9.peg.1037; -.
DR   eggNOG; COG0404; Bacteria.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_11_0_5; -.
DR   Proteomes; UP000000552; Chromosome.
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; 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;
FT   DOMAIN          9..373
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          377..431
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          434..703
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          728..806
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   817 AA;  91260 MW;  D6CEE09964D162EF CRC64;
     MAGLPSTARV VIIGGGVVGT SSLYHLAKAG WTDCVLLEKN ELTSGSTWHA AGNVPTFSSS
     WSLMNMQRYS TELYRGLADA VDYPMNYHVT GSLRLAHTKE RMQEFQRAKG MGRYQGMDID
     VVGVDEIKRR YPFIETHDLK GALYDPSDGD IDPAQLTQAL AKGARDLGAK IIRFCPVTGV
     RREKDEWVVT TPQGEIRCEI VVNAAGYRAA EVGRMFGREV PMMVMSHQYI LFEEIPELAA
     WSKEQGKKLP LLRDVDTSYY LRQEKAGMNL GPYERNCRAH WATPGDPMPE DFSFQLFPDD
     LDRLEHYLAD AVARVPILGT AGLSKVINGP IPYAPDGNPL IGPMPGVPNA FEACVFTFGI
     AQGGGAGKVL AEWVTQGQTE WDMWSCDPRR FTSFASAPDY CVAKGMEIYG NEYAIQFPRH
     AWPEGRDRKL SPIHDRTKAL GGRFDAYNGW ERATWYAKDG DDISEEATLT FRRDGPWQHR
     VREECLAVRD AAGILDLPGF SRFRLQGPGA RDWLATMITG LVPKPGRIGL GYFSDDKGRI
     VTEMSIMALA EDLFFLITAS VAEQHDFEWL QYHLPQPNEL TLQNLTEAFS CQILSGPKSR
     DILSELTAAD LSLPWLSHQS VQISGHWCQL VRVSFVGELG WEIHTKVDDT AAVFDAVWAA
     GQKHGLKPFG MYALDSLRLE KGYRTWKGDL STDYSILQGG LERFVKWEKP DFRGKAALQN
     EKQQGVKKRF VTLVVENPGD CDAPYMSTLW HGGQIVGETT SGGWGHRIDK SIALGMLRVD
     LTEPGTSVEV EIFGDRFQAV VQKDEPLWDP RNERLRA
//
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