ID H2L0N9_CAEEL Unreviewed; 830 AA.
AC H2L0N9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Dimethylglycine dehydrogenase, mitochondrial {ECO:0000313|EMBL:CCD73437.1};
GN ORFNames=CELE_Y37E3.17 {ECO:0000313|EMBL:CCD73437.1}, Y37E3.17
GN {ECO:0000313|EMBL:CCD73437.1, ECO:0000313|WormBase:Y37E3.17a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD73437.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD73437.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD73437.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; BX284601; CCD73437.1; -; Genomic_DNA.
DR RefSeq; NP_001021745.1; NM_001026574.3.
DR AlphaFoldDB; H2L0N9; -.
DR SMR; H2L0N9; -.
DR EPD; H2L0N9; -.
DR PeptideAtlas; H2L0N9; -.
DR EnsemblMetazoa; Y37E3.17a.1; Y37E3.17a.1; WBGene00021355.
DR GeneID; 171775; -.
DR AGR; WB:WBGene00021355; -.
DR WormBase; Y37E3.17a; CE30219; WBGene00021355; -.
DR HOGENOM; CLU_007884_11_0_1; -.
DR OrthoDB; 1815533at2759; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00021355; Expressed in larva and 4 other cell types or tissues.
DR ExpressionAtlas; H2L0N9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0047865; F:dimethylglycine dehydrogenase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|EPD:H2L0N9,
KW ECO:0007829|PeptideAtlas:H2L0N9};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 31..392
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 395..444
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 451..714
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 754..824
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 830 AA; 91822 MW; 452A8DF37DE44B2E CRC64;
MLHASRSLIR TSSDLHTSIR NSSSTKHVFA CVLGSGVAGS SVAYHLTKRN IKDVLLLERA
SGVASPSGTS FHSPGLVSAS HPAHRYKPIL AHSIELYSKL EAETGVNIDF QPTGTIRLAT
NETRLAEFRK YVNRDYYKEG DVCKTTLLTP DQVRELAPDV DHSKILGALH TTNDGTISAR
ALTQALVVGA KNGGAQVIDG AIPKEIKYDK EKGHWIIALE DGTLVTTRNL INAGGIWAND
IARLSGHALP VVVVEHQYAV LTPNKTPGPT PAIIDHDSTF YVRKSGDDYL FGGFESLEKT
VIREDWYKKG VPTEGSKSIQ ADFSRLDDAY KRACDLIPGL QGSKVDARAA VFSMTPDGYP
LVGPYDKNYW MSTGFLDGVS SGGGIGKYLA DWIVDGEPPA ELFDTDASRY ERWGDRKFFT
ERSRETYSMY YNWSYTDRSA GRPTDRISGV YGRLKKDGAS FSFRNGWEVA NSFNMGVQNE
EYLPTLIREY EMVTNKCGVI DLSWKGKIEV KGNDAEKLMD YAIASQIPAL GKISSGLMLT
RHGGILGPMM IFHHDRQRSA FILLTEPERE SRDLYWLRRA AAEKKFDVQV SIVSEYLASL
ALVGPKSREV LSALTKSDVS DEGFPQKSTR MIRLGPVGVV CARSSTSTGQ LSYELFHNRA
ETAKLYNAVM SAGREHGIVN FGQAALNMMR LEHGYKIWGK ELTLDTNPFE CGIGGLVDFE
KKEFIGRESA LELKKKDFDR RLALITFDTE EGCVLDDRYV PSGNEVIRID GKEARVGQIT
SGAYNVRLQK PIAFAWIDNA VGKNERLVVD IGDKRLFATS LETPTIPPIQ
//
