ID A0A1X7H1A2_9PROT Unreviewed; 809 AA.
AC A0A1X7H1A2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|EMBL:SMF77880.1};
GN ORFNames=SAMN02744631_0863 {ECO:0000313|EMBL:SMF77880.1};
OS Candidatus Pelagibacter sp. HIMB1321.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae; Pelagibacter.
OX NCBI_TaxID=1388755 {ECO:0000313|EMBL:SMF77880.1, ECO:0000313|Proteomes:UP000192921};
RN [1] {ECO:0000313|Proteomes:UP000192921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB1321 {ECO:0000313|Proteomes:UP000192921};
RA Varghese N., Submissions S.;
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; LT840186; SMF77880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7H1A2; -.
DR STRING; 1388755.SAMN02744631_0863; -.
DR OrthoDB; 9804379at2; -.
DR Proteomes; UP000192921; Chromosome i.
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;
FT DOMAIN 10..368
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 371..425
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 428..695
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 723..801
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 809 AA; 91491 MW; 367F9F0BA38B7732 CRC64;
MSELQSHAKL VIIGGGIMGV SLLYHLTKEG WSDVVLIEKS ELTSGSTWHA AGQCPHMLSS
LNLAKIHLHS TNLYKSLEKE TGQPTGFHET GSLRLAYKKE DLQWFHYVKG ILDIAGSPCS
IISTDEIHKY HPFIKLDGIL GAFYTPEDGY TDPTSTTNAM AKGARDKGAK IYRKNRVTDI
EQLPSGEWKV ITEKGNITCE HVVNAAGSFC PEVSQMVGIK NVPSINMVHQ YLVTEAHPEI
EKLDKELPVV RDPDSSSYLR QEGKGLLIGP YEKEVAAWAL EGMDWKFDME LLEPDLDRIE
KYLERGMDRI PQFKDVGIKR IICGPITHTP DDNFLAGPAP GLKNFWMFCA ASIGIAHGGG
AGKFMAQWIV HGDSEINMME FEPRRYLNWV DKEYSVIKSK EQYGRMYITP MPHEKVEAGR
PMKTSGVYQT LKDKGAEYYD LYGWEKPDWF NTDKIKEELS YNRNNVFPYI QKECEHVHNH
VGILDLSTFS KYEITGEDSY QFLDRLCVNR IPKKDGSIIL THTLNNIGRI QSEFTITKVK
ENHYYALSAA VSEIRDLDWF NQNKLDTEKV AIKNVSLEKG VLGLIGPKSR NVLSKVTNTD
LSNENFPWLK SKQIKINDIE VLALRVNYAG ELGWELHIAM DKMSEVYDLL FKEGQSENII
DFGSRTLNSM RMEKGYRGWG SELTPEISVV EASLDKFFNL DKKDNFIGSD AVKERLKKGI
DTKLVYLEVD AKNADAHGNE PVYFNNERVG LTTSGGYGFR VKKSLAFAYV KPETAKLGNE
FTIEIQGNKI KATIIKEPVF DPENNKLKA
//
