ID A0A3B4U430_SERDU Unreviewed; 870 AA.
AC A0A3B4U430;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|Ensembl:ENSSDUP00000013359.1};
GN Name=DMGDH {ECO:0000313|Ensembl:ENSSDUP00000013359.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000013359.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000013359.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR AlphaFoldDB; A0A3B4U430; -.
DR STRING; 41447.ENSSDUP00000013359; -.
DR Ensembl; ENSSDUT00000013603.1; ENSSDUP00000013359.1; ENSSDUG00000009692.1.
DR GeneTree; ENSGT00940000158176; -.
DR OMA; NGWERPN; -.
DR OrthoDB; 1815533at2759; -.
DR Proteomes; UP000261420; Unplaced.
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 57..419
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 422..473
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 483..749
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 775..852
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 870 AA; 96563 MW; EDBD226C31008F07 CRC64;
MSRILNLIKV QLRRDLAAHG GTARLPLRTI CCTARKQAEE SDASTVLGKR WKDTAETVII
GGGCVGVSLA YHLAKAGMKD VVLLEKSELT AGSTWHAAGL TTYYHPGINL KKVHYDSIKL
YERLEAETGQ AVGFHQPGSV RIASTAARVD EMKYQMTRTH WHVTPQYLIG PEKVQEYFPL
INIDKVLAGL YTPGDGHIDP YSLTMALAAG ARMYGAQIYN PAPVTALNPT ADGKWDVQTP
HGTIRANRIV NATGFWAREV GKMIGFDHPT IPVHHQYVVT ATVPEVKALK KEVAVIRDLE
GSYYLRQERD GLLFGPYEKM EKMVLQDSWV RDGVPPGFGK ELFESDLDRI MEHVEMAMEM
VPVLKKADII NIVSGPITYT PDLLPMVGPH QGVRNYWTAI GFGYGVIHAG GIGKFLSDWI
VNGEPPYDLI ECDPNRYGKW TDVPFMCAKA RESYGFNNVV GYPKEERFAG RPTIRTSGIY
ELLKDKASMG FHAGWEQPHW FYKPGDDTGY KPSFRRTNWF GPVGRECRLV MEKVGVIDLT
PFGKFVVKGK DSHKLLDRLF ANTMPKVGIT NISHMLTPTG RVYAEVTITQ LAPGEFLLIT
GSGSELHDLR WIETEAADGG YDVDISNVTE DIGVLGIAGP NSRKVLQKLT EEDMSDAGFK
FLHCKSIKLA GIPVRAIRIS YTGELGWELY IDQKNMAAVY QAMMEAGKDE GIDNFGTYAM
SSLRLEKGFR GWGAEMNCDT NPLEAGLDYF IKLNKPADFI GKAALQQIKA KGLKRKLSYI
TLDTDDIDPE GNETIWHNGK VVGNTTSGAY SYSSQQSLAF AYLPVELCSV GQKVEVELLG
RKYPAMVIQE PLVLTEPTRT RLQKKAKGKA
//
