ID G3WQF5_SARHA Unreviewed; 872 AA.
AC G3WQF5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Dimethylglycine dehydrogenase {ECO:0000313|Ensembl:ENSSHAP00000017660.2};
GN Name=DMGDH {ECO:0000313|Ensembl:ENSSHAP00000017660.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000017660.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000017660.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000017660.2}
RP IDENTIFICATION.
RG Ensembl;
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_003759482.1; XM_003759434.2.
DR AlphaFoldDB; G3WQF5; -.
DR Ensembl; ENSSHAT00000017805.2; ENSSHAP00000017660.2; ENSSHAG00000014992.2.
DR GeneID; 100931635; -.
DR KEGG; shr:100931635; -.
DR CTD; 29958; -.
DR GeneTree; ENSGT00940000158176; -.
DR HOGENOM; CLU_007884_11_1_1; -.
DR InParanoid; G3WQF5; -.
DR OMA; NGWERPN; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0047865; F:dimethylglycine dehydrogenase activity; IEA:Ensembl.
DR GO; GO:0042426; P:choline catabolic process; IEA:Ensembl.
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:UP000007648}.
FT DOMAIN 58..420
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 424..476
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 486..750
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 776..854
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 872 AA; 97517 MW; 40C8EEB405C4451E CRC64;
MLLGGLRHLR FQLRKTESTL TPGIRLRSVC SSSGLPFQEG GGKAPSFSET RWKDTAETVI
IGGGCVGVSL AYHLAKAGMK DVVLLEASEL TAGSTWHAAG LTTYFHPGIN LKKIHYYSIK
LYEKLEEETG QVVGFHQPGS IRLATTPTRV DEFKYQMTRT RWHATEQYLI EPEKVQEMFP
LLNMEKVLAG LYNPGDGHID PYSLTMALAA GARKYGALLK FPARVTNLKP RSDGTWEVET
PQGSIQANRI VNATGFWARE VGKLIGLEHP LIPVHHQYVV TATIPEVKAL KRELPVLRDL
EGSYYLRQER DGLLFGPYES QEKMKVQDSW VINGVPPGFG KELFESDLDR IMEHVEAAMD
MVPVLRKADI INIVSGPITY SPDILPMVGP HQGVRNYWVA IGFGYGIIHA GGVGKYLSDW
ILSGEPPFDL IELDPNRYGK WTTTQYTETK ARESYGFNNI VGYPKEERFA GRPTKRISGI
YNILKSKCSM GFHAGWEQPH WFYKPGQEPG YKPSFRRTNW FQPVGSEYQQ VMQKVGVIDL
TPFGKFKVRG KDSLKLLDRL FANVIPKVGF TNISHMLTPK GRVYAELTVC QQSPGEFLLI
TGSGSELHDL RWIEEEIVKG GYDVEIENIT DELGVLGVAG PSARSVLQKL TSADLSNDAF
KFLQSKPLTI SNIPVTAIRI SYTGELGWEL YHRQEDSAML YGAIMEAGQE EGIDNFGTYA
MNALRMEKAF RAWGSEMNCD TNPLEAGLDH FIKLNKPADF IGKQALKQMK EKGLKRRLVY
LTLETDHVDP EGNESIWHDG KVVGNTTSGS YSYSVQKSLA FAYVPMELSK MGQKVEVELL
GKNYPATIIQ EPLVLTEPTR ARLQKKAGNS QV
//
