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Protein

Dimethylglycine dehydrogenase, mitochondrial

Gene

Dmgdh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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

FAD1 PublicationNote: Binds 1 FAD covalently per monomer.1 Publication

Pathway:ibetaine 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

  • dimethylglycine dehydrogenase activity Source: RGD
  • flavin adenine dinucleotide binding Source: RGD
  • folic acid binding Source: RGD

GO - Biological processi

  • amino-acid betaine catabolic process Source: UniProtKB-UniPathway
  • choline catabolic process Source: RGD
  • choline metabolic process Source: RGD
  • tetrahydrofolate interconversion Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16117.
BRENDAi1.5.8.4. 5301.
UniPathwayiUPA00291; UER00433.

Names & Taxonomyi

Protein namesi
Recommended name:
Dimethylglycine dehydrogenase, mitochondrial (EC:1.5.8.4)
Alternative name(s):
ME2GLYDH
Gene namesi
Name:Dmgdh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620453. Dmgdh.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343MitochondrionSequence AnalysisAdd
BLAST
Chaini44 – 857814Dimethylglycine dehydrogenase, mitochondrialPRO_0000010769Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ63342.
PRIDEiQ63342.

PTM databases

PhosphoSiteiQ63342.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000030481.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 488Combined sources
Helixi52 – 6312Combined sources
Beta strandi68 – 725Combined sources
Beta strandi74 – 763Combined sources
Turni77 – 815Combined sources
Helixi82 – 843Combined sources
Beta strandi94 – 963Combined sources
Helixi98 – 11619Combined sources
Beta strandi127 – 1315Combined sources
Helixi134 – 14714Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi155 – 1573Combined sources
Helixi159 – 1657Combined sources
Beta strandi176 – 1805Combined sources
Helixi188 – 20114Combined sources
Beta strandi205 – 2095Combined sources
Beta strandi214 – 2174Combined sources
Beta strandi223 – 2275Combined sources
Beta strandi230 – 23910Combined sources
Helixi242 – 2443Combined sources
Helixi245 – 2506Combined sources
Turni251 – 2533Combined sources
Beta strandi259 – 26810Combined sources
Helixi272 – 2754Combined sources
Beta strandi283 – 2864Combined sources
Turni287 – 2904Combined sources
Beta strandi291 – 2966Combined sources
Beta strandi299 – 3046Combined sources
Turni308 – 3103Combined sources
Helixi315 – 3206Combined sources
Helixi336 – 3383Combined sources
Helixi339 – 34810Combined sources
Helixi350 – 3534Combined sources
Beta strandi357 – 36711Combined sources
Beta strandi374 – 3774Combined sources
Beta strandi384 – 3885Combined sources
Helixi393 – 41018Combined sources
Helixi418 – 4203Combined sources
Helixi422 – 4243Combined sources
Helixi431 – 44313Combined sources
Turni444 – 4463Combined sources
Helixi467 – 4715Combined sources
Turni472 – 4743Combined sources
Beta strandi475 – 4806Combined sources
Beta strandi483 – 4897Combined sources
Helixi508 – 52013Combined sources
Beta strandi523 – 5264Combined sources
Beta strandi530 – 5378Combined sources
Helixi540 – 5478Combined sources
Beta strandi548 – 5503Combined sources
Beta strandi557 – 5648Combined sources
Beta strandi570 – 58011Combined sources
Beta strandi583 – 5886Combined sources
Helixi590 – 5923Combined sources
Helixi593 – 60614Combined sources
Beta strandi612 – 6154Combined sources
Turni617 – 6193Combined sources
Beta strandi620 – 6278Combined sources
Helixi630 – 6356Combined sources
Turni644 – 6463Combined sources
Beta strandi651 – 6577Combined sources
Beta strandi660 – 6656Combined sources
Beta strandi671 – 68010Combined sources
Helixi681 – 6833Combined sources
Helixi684 – 69411Combined sources
Turni695 – 6995Combined sources
Helixi705 – 71410Combined sources
Turni720 – 7223Combined sources
Turni730 – 7345Combined sources
Helixi736 – 7383Combined sources
Beta strandi743 – 7453Combined sources
Helixi750 – 75910Combined sources
Beta strandi762 – 7709Combined sources
Beta strandi782 – 7854Combined sources
Beta strandi788 – 79912Combined sources
Turni800 – 8034Combined sources
Beta strandi804 – 8129Combined sources
Helixi813 – 8153Combined sources
Beta strandi821 – 8266Combined sources
Beta strandi829 – 8357Combined sources
Helixi844 – 85714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P9SX-ray2.32A/B22-857[»]
4PAAX-ray2.26A/B22-857[»]
4PABX-ray1.85A/B2-857[»]
ProteinModelPortaliQ63342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GcvT family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0665.
HOGENOMiHOG000251716.
HOVERGENiHBG081945.
InParanoidiQ63342.
PhylomeDBiQ63342.

Family and domain databases

Gene3Di2.40.30.110. 1 hit.
3.30.1360.120. 2 hits.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR013977. GCV_T_C.
IPR006222. GCV_T_N.
IPR029043. GcvT/YgfZ_C.
IPR027266. TrmE/GcvT_dom1.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
PF01571. GCV_T. 1 hit.
PF08669. GCV_T_C. 1 hit.
[Graphical view]
SUPFAMiSSF101790. SSF101790. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q63342-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRLGALRLR GLALRSSQGR PSSAGLREGQ ESPPSPPEWK DRAETVIIGG
60 70 80 90 100
GCVGVSLAYH LAKAGMRDVV LLEKSELTAG STWHAAGLTT YFHPGINLKK
110 120 130 140 150
IHYDSIKLYE RLEEETGQVV GFHQPGSIRL ATTPERVDEF KYQMTRTNWH
160 170 180 190 200
ATEQYIIEPE KIHELFPLLN MDKILAGLYN PGDGHIDPYS LTMALATGAR
210 220 230 240 250
KYGVLLKYPA PVTSLKPRPD GTWDVETPQG SVRANRIVNA AGFWAREVGK
260 270 280 290 300
MIGLDHPLIP VQHQYVVTST IPEVKALKRE LPVLRDLEGS YYLRQERDGL
310 320 330 340 350
LFGPYESQEK MKLQASWVAH GVPPGFGKEL FESDLDRITE HVEAAMEMVP
360 370 380 390 400
VLKKADIINI VNGPITYSPD ILPMVGPHQG VRNYWVAIGF GYGIIHAGGV
410 420 430 440 450
GKYLSDWILH GEPPFDLIEL DPNRYGKWTT TQYTEAKARE SYGFNNIVGY
460 470 480 490 500
PKEERFAGRP TQRVSGLYKI LESKCSMGFH AGWEQPHWFY KPGQDTQYRP
510 520 530 540 550
SFRRTNWFRP VGSEYKQVMQ RVGVIDLSPF GKFNIKGQDS TQLLDHLCAN
560 570 580 590 600
VIPKVGFTNI SHMLTPRGRV YAELTVSHQS PGEFLLITGS GSELHDLRWI
610 620 630 640 650
EEAAVRGGYD VEIRNITDEL GVLGVAGPYA RRVLQKLTSE DLSDDVFKFL
660 670 680 690 700
QTKSLKISDI PVTAIRISYT GELGWELYHR REDSAALYER IMNAGQEEGI
710 720 730 740 750
DNFGTYALNA LRLEKAFRAW GSEMNCDTNP LEAGLDYFIK LNKPADFTGK
760 770 780 790 800
QALKQIKAKG LKRRLVCLTL ATDDVDPEGN ESVWYKGKVI GNTTSGSYSY
810 820 830 840 850
SIQKSLAFAY VPVELSEVGQ QVEVELLGKN YPATIIQEPL VLTEPTRTRL

QKDGRKS
Length:857
Mass (Da):96,048
Last modified:November 1, 1996 - v1
Checksum:iA6FED946B8AB9878
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55995 mRNA. Translation: CAA39468.1.
PIRiS16133.
UniGeneiRn.3646.

Genome annotation databases

UCSCiRGD:620453. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55995 mRNA. Translation: CAA39468.1.
PIRiS16133.
UniGeneiRn.3646.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P9SX-ray2.32A/B22-857[»]
4PAAX-ray2.26A/B22-857[»]
4PABX-ray1.85A/B2-857[»]
ProteinModelPortaliQ63342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000030481.

PTM databases

PhosphoSiteiQ63342.

Proteomic databases

PaxDbiQ63342.
PRIDEiQ63342.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:620453. rat.

Organism-specific databases

RGDi620453. Dmgdh.

Phylogenomic databases

eggNOGiCOG0665.
HOGENOMiHOG000251716.
HOVERGENiHBG081945.
InParanoidiQ63342.
PhylomeDBiQ63342.

Enzyme and pathway databases

UniPathwayiUPA00291; UER00433.
BioCyciMetaCyc:MONOMER-16117.
BRENDAi1.5.8.4. 5301.

Miscellaneous databases

PROiQ63342.

Family and domain databases

Gene3Di2.40.30.110. 1 hit.
3.30.1360.120. 2 hits.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR013977. GCV_T_C.
IPR006222. GCV_T_N.
IPR029043. GcvT/YgfZ_C.
IPR027266. TrmE/GcvT_dom1.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
PF01571. GCV_T. 1 hit.
PF08669. GCV_T_C. 1 hit.
[Graphical view]
SUPFAMiSSF101790. SSF101790. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Rat liver dimethylglycine dehydrogenase. Flavinylation of the enzyme in hepatocytes in primary culture and characterization of a cDNA clone."
    Lang H., Polster M., Brandsch R.
    Eur. J. Biochem. 198:793-799(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Liver.
  2. "The amino acid sequences of the flavin-peptides of dimethylglycine dehydrogenase and sarcosine dehydrogenase from rat liver mitochondria."
    Cook R.J., Misono K.S., Wagner C.
    J. Biol. Chem. 260:12998-13002(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: FAD-BINDING.
    Tissue: Liver.

Entry informationi

Entry nameiM2GD_RAT
AccessioniPrimary (citable) accession number: Q63342
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 117 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.