ID A0A1S3LRM7_SALSA Unreviewed; 868 AA.
AC A0A1S3LRM7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Dimethylglycine dehydrogenase, mitochondrial {ECO:0000313|RefSeq:XP_013993633.1};
GN Name=dmgdh {ECO:0000313|RefSeq:XP_013993633.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013993633.1};
RN [1] {ECO:0000313|RefSeq:XP_013993633.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013993633.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR RefSeq; XP_013993633.1; XM_014138158.1.
DR AlphaFoldDB; A0A1S3LRM7; -.
DR STRING; 8030.ENSSSAP00000116671; -.
DR PaxDb; 8030-ENSSSAP00000116671; -.
DR KEGG; sasa:106568126; -.
DR OrthoDB; 1815533at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 57..419
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 422..475
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 485..749
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 775..853
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 868 AA; 96597 MW; C3C0978CDBF8D450 CRC64;
MSRFFNAINT HLRRDLAAYR AIVCLPLRTI NYTSQKHVGN GDSTMVLGKR WKDTAETVII
GGGCVGVSLA YHLAKAGQKD VVLLEKSELT AGSTWHAAGL TTYYHPGINL KKVHYHSIKL
YESLEAETGQ AVGFHQPGSI RIASTPVRVD ELKYQMARAH WHPTPQWLIT PEKIKELFPL
LNMDKVLAGL YNPGDGHIDP YSLTMALAAG ARMYGAQIYN PALVSGLTPT SDGKWDVQTP
YGTIRANRIV NATGFWAREV GQQIGFEHPT IPVHHQYVVT ATVPEVKALK TELPVIRDLE
GSYYLRQERD GLLFGPYERE EKMVLQDSWV RDGVPPGFGK ELFESDLDRI MHHVEMAMEM
VPVLKNADII NIVSGPITYT PDLLPMVGPH QGARSYWTAI GFGYGVIHAG GIGKFLSDWI
VTGEPPYDLI ECDPNRYGKW TTVPYMCAKA RESYGFNNVV GYPKEERFAG RPTNRTSGVY
ELLKGKASMG FHAGWEQPHW FYKPGDDAGY KPSFRRTNWF GPVGRECKLV MEKVGVIDLT
PFGKFMVKGK DSHKLLDRLF ANTMPKVGLT NISHMLTPTG RVYAEVTITQ LTTGEFLLIT
GSGSELHDLR WMEEVVVEGA YDVDISNVTE DIGVLGVAGP KARDVLQKLT QEDMSDASFK
FLHCKPIQLG GVNLRAIRIS YTGELGWELY IPHKDMAAVY QAIMAAGEDE GIDNFGTYAM
SSLRLEKGFR GWGAEMNCDT NPLEAGLDYF IKLNKHADFI GKAALQEIKA KGLKRKLSYI
TMDTDDVDPE GNETIWLNGK VVGNTTSGAY SYTTQQSLAF AYLPVELCSV GQKVEVEMLG
RKYPAMVVQE PLVLTEPTRT RLQKKSKA
//