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Protein

Dimethylglycine dehydrogenase, mitochondrial

Gene

Dmgdh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

N,N-dimethylglycine + electron-transfer flavoprotein + H2O = sarcosine + formaldehyde + reduced electron-transfer flavoprotein.

Cofactori

FADBy similarityNote: Binds 1 FAD covalently per monomer.By similarity

Pathwayi: betaine degradation

This protein is involved in step 2 of the subpathway that synthesizes sarcosine from betaine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Betaine--homocysteine S-methyltransferase 1 (Bhmt)
  2. Dimethylglycine dehydrogenase, mitochondrial (Dmgdh)
This subpathway is part of the pathway betaine degradation, which is itself part of Amine and polyamine degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sarcosine from betaine, the pathway betaine degradation and in Amine and polyamine degradation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.5.8.4. 3474.
ReactomeiR-MMU-6798163. Choline catabolism.
UniPathwayiUPA00291; UER00433.

Names & Taxonomyi

Protein namesi
Recommended name:
Dimethylglycine dehydrogenase, mitochondrial (EC:1.5.8.4)
Alternative name(s):
ME2GLYDH
Gene namesi
Name:Dmgdh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1921379. Dmgdh.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343MitochondrionSequence analysisAdd
BLAST
Chaini44 – 869826Dimethylglycine dehydrogenase, mitochondrialPRO_0000010768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 841Tele-8alpha-FAD histidineBy similarity
Modified residuei107 – 1071N6-acetyllysineCombined sources
Modified residuei141 – 1411N6-acetyllysine; alternateCombined sources
Modified residuei141 – 1411N6-succinyllysine; alternateCombined sources
Modified residuei161 – 1611N6-acetyllysineCombined sources
Modified residuei216 – 2161N6-acetyllysineCombined sources
Modified residuei310 – 3101N6-succinyllysineCombined sources
Modified residuei312 – 3121N6-succinyllysineCombined sources
Modified residuei328 – 3281N6-acetyllysineCombined sources
Modified residuei353 – 3531N6-acetyllysineCombined sources
Modified residuei427 – 4271N6-acetyllysine; alternateCombined sources
Modified residuei427 – 4271N6-succinyllysine; alternateCombined sources
Modified residuei469 – 4691N6-acetyllysine; alternateCombined sources
Modified residuei469 – 4691N6-succinyllysine; alternateCombined sources
Modified residuei516 – 5161N6-acetyllysine; alternateCombined sources
Modified residuei516 – 5161N6-succinyllysine; alternateCombined sources
Modified residuei648 – 6481N6-acetyllysine; alternateCombined sources
Modified residuei648 – 6481N6-succinyllysine; alternateCombined sources
Modified residuei757 – 7571N6-acetyllysineCombined sources
Modified residuei786 – 7861N6-acetyllysine; alternateCombined sources
Modified residuei786 – 7861N6-succinyllysine; alternateCombined sources
Modified residuei788 – 7881N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9DBT9.
MaxQBiQ9DBT9.
PaxDbiQ9DBT9.
PRIDEiQ9DBT9.

PTM databases

iPTMnetiQ9DBT9.
PhosphoSiteiQ9DBT9.
SwissPalmiQ9DBT9.

Expressioni

Gene expression databases

BgeeiQ9DBT9.
CleanExiMM_DMGDH.
GenevisibleiQ9DBT9. MM.

Interactioni

Protein-protein interaction databases

IntActiQ9DBT9. 2 interactions.
MINTiMINT-1840379.
STRINGi10090.ENSMUSP00000039663.

Structurei

3D structure databases

ProteinModelPortaliQ9DBT9.
SMRiQ9DBT9. Positions 38-857.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GcvT family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2844. Eukaryota.
COG0404. LUCA.
COG0665. LUCA.
GeneTreeiENSGT00530000063120.
HOGENOMiHOG000251716.
HOVERGENiHBG081945.
InParanoidiQ9DBT9.
KOiK00315.
OMAiYESQEKM.
OrthoDBiEOG7CCBQB.
PhylomeDBiQ9DBT9.
TreeFamiTF314735.

Family and domain databases

Gene3Di2.40.30.110. 1 hit.
3.30.1360.120. 2 hits.
3.50.50.60. 3 hits.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR032503. FAO_M.
IPR013977. GCV_T_C.
IPR006222. GCV_T_N.
IPR029043. GcvT/YgfZ_C.
IPR027266. TrmE/GcvT_dom1.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
PF16350. FAO_M. 1 hit.
PF01571. GCV_T. 1 hit.
PF08669. GCV_T_C. 1 hit.
[Graphical view]
SUPFAMiSSF101790. SSF101790. 1 hit.
SSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9DBT9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRPGALRLR GLALRGSPRR PSSAGLREGQ ESPASPPEWK DRAETVIIGG
60 70 80 90 100
GCVGVSLAYH LAKAGMRDVV LMEKSELTAG STWHAAGLTT YFHPGINLKK
110 120 130 140 150
IHYDSIKLYE RLEEETGQVV GFHQPGSIRL ATTPVRVDEF KYQMTRTNWH
160 170 180 190 200
ATEQYIIEPE KIHELFPLLN MNKILAGLYN PGDGHIDPYS LTMALAAGAR
210 220 230 240 250
KYGALLKYPA PVTSLKPRPD GTWDVETPQG SVRANRIVNA AGFWAREVGK
260 270 280 290 300
MIGLDHPLIP VQHQYVVTST IPEVKALKRE LPVLRDLEGS YYLRQERDGL
310 320 330 340 350
LFGPYESQEK MKLQASWVTH GVPPGFGKEL FESDLDRISD HLEAAMEMIP
360 370 380 390 400
VLKKADIINV VNGPITYSPD ILPMVGPHQG VRNYWVATGF GYGIIHAGGV
410 420 430 440 450
GKFLSDWILH GEPPFDLIEL DPNRYGKWTT TQYTEAKARE SYGFNNIVGY
460 470 480 490 500
PKEERFAGRP TQRVSGLYKT LKSKCSMGFH AGWEQPHWFY KPGQDTQYRP
510 520 530 540 550
SFRRTNWFEP VGSEYKQVMQ RVGVIDLSPF GKFNIKGRDS TQLLDHLFAN
560 570 580 590 600
VIPKVGFTNI SHMLTPRGRV YAELTVSQQS PGEFLLITGS GSELHDLRWI
610 620 630 640 650
EEAAFRGGYD VEIQNITDEF GVLGVAGPYA RRVLQKLTSE DLSDDAFKFL
660 670 680 690 700
QTKSFNISDI PVTAIRISYT GELGWELYHR REDSATLYER IMSAGQEEGI
710 720 730 740 750
GDFGTYALNA LRLEKAFRAW GSEMNCDTNP LEAGLEYFVK LNKPADFIGK
760 770 780 790 800
QALKQIKTEG LKRRLVCLTV ATDDVDPEGN ESIWYKGKVV GNTTSGSYSY
810 820 830 840 850
SIQKSLAFAY VPVQLSEVGQ QVEVELLGKN YPATIIQEPL VLTEPARARL
860
QKDGKKTNLE KGPSRTTKL
Length:869
Mass (Da):97,255
Last modified:June 1, 2001 - v1
Checksum:iD415C743105A0547
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti758 – 7581T → A in AAH24126 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004755 mRNA. Translation: BAB23536.1.
CT030023, AC131739 Genomic DNA. Translation: CAO77970.1.
BC024126 mRNA. Translation: AAH24126.1.
CCDSiCCDS26690.1.
RefSeqiNP_083048.1. NM_028772.3.
UniGeneiMm.21789.

Genome annotation databases

EnsembliENSMUST00000048001; ENSMUSP00000039663; ENSMUSG00000042102.
GeneIDi74129.
KEGGimmu:74129.
UCSCiuc007rll.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004755 mRNA. Translation: BAB23536.1.
CT030023, AC131739 Genomic DNA. Translation: CAO77970.1.
BC024126 mRNA. Translation: AAH24126.1.
CCDSiCCDS26690.1.
RefSeqiNP_083048.1. NM_028772.3.
UniGeneiMm.21789.

3D structure databases

ProteinModelPortaliQ9DBT9.
SMRiQ9DBT9. Positions 38-857.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DBT9. 2 interactions.
MINTiMINT-1840379.
STRINGi10090.ENSMUSP00000039663.

PTM databases

iPTMnetiQ9DBT9.
PhosphoSiteiQ9DBT9.
SwissPalmiQ9DBT9.

Proteomic databases

EPDiQ9DBT9.
MaxQBiQ9DBT9.
PaxDbiQ9DBT9.
PRIDEiQ9DBT9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048001; ENSMUSP00000039663; ENSMUSG00000042102.
GeneIDi74129.
KEGGimmu:74129.
UCSCiuc007rll.1. mouse.

Organism-specific databases

CTDi29958.
MGIiMGI:1921379. Dmgdh.

Phylogenomic databases

eggNOGiKOG2844. Eukaryota.
COG0404. LUCA.
COG0665. LUCA.
GeneTreeiENSGT00530000063120.
HOGENOMiHOG000251716.
HOVERGENiHBG081945.
InParanoidiQ9DBT9.
KOiK00315.
OMAiYESQEKM.
OrthoDBiEOG7CCBQB.
PhylomeDBiQ9DBT9.
TreeFamiTF314735.

Enzyme and pathway databases

UniPathwayiUPA00291; UER00433.
BRENDAi1.5.8.4. 3474.
ReactomeiR-MMU-6798163. Choline catabolism.

Miscellaneous databases

PROiQ9DBT9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBT9.
CleanExiMM_DMGDH.
GenevisibleiQ9DBT9. MM.

Family and domain databases

Gene3Di2.40.30.110. 1 hit.
3.30.1360.120. 2 hits.
3.50.50.60. 3 hits.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR032503. FAO_M.
IPR013977. GCV_T_C.
IPR006222. GCV_T_N.
IPR029043. GcvT/YgfZ_C.
IPR027266. TrmE/GcvT_dom1.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
PF16350. FAO_M. 1 hit.
PF01571. GCV_T. 1 hit.
PF08669. GCV_T_C. 1 hit.
[Graphical view]
SUPFAMiSSF101790. SSF101790. 1 hit.
SSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 237-869.
    Tissue: Liver.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Liver.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-141; LYS-310; LYS-312; LYS-427; LYS-469; LYS-516; LYS-648; LYS-786 AND LYS-788, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-107; LYS-141; LYS-161; LYS-216; LYS-328; LYS-353; LYS-427; LYS-469; LYS-516; LYS-648; LYS-757 AND LYS-786, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiM2GD_MOUSE
AccessioniPrimary (citable) accession number: Q9DBT9
Secondary accession number(s): B1B1D0, Q8R1S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.