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Q32LG3 (MDHM_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Malate dehydrogenase, mitochondrial

EC=1.1.1.37
Gene names
Name:MDH2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH.

Enzyme regulation

Enzyme activity is enhanced by acetylation By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Post-translational modification

Acetylation is enhanced by up to 67% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with the appearance of tri-and tetraacetylations. Glucose also increases acetylation by about 60% By similarity. Ref.2

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion By similarity
Chain25 – 338314Malate dehydrogenase, mitochondrial
PRO_0000260267

Regions

Nucleotide binding31 – 377NAD By similarity
Nucleotide binding140 – 1423NAD By similarity

Sites

Active site2001Proton acceptor By similarity
Binding site571NAD By similarity
Binding site1041Substrate By similarity
Binding site1101Substrate By similarity
Binding site1171NAD By similarity
Binding site1421Substrate By similarity
Binding site1761Substrate By similarity
Binding site2511NAD By similarity

Amino acid modifications

Modified residue781N6-acetyllysine; alternate By similarity
Modified residue781N6-succinyllysine; alternate By similarity
Modified residue911N6-acetyllysine; alternate By similarity
Modified residue911N6-succinyllysine; alternate By similarity
Modified residue1651N6-acetyllysine By similarity
Modified residue1851N6-acetyllysine; alternate Ref.2
Modified residue1851N6-succinyllysine; alternate By similarity
Modified residue2031N6-succinyllysine By similarity
Modified residue2151N6-acetyllysine; alternate By similarity
Modified residue2151N6-succinyllysine; alternate By similarity
Modified residue2391N6-acetyllysine; alternate By similarity
Modified residue2391N6-malonyllysine; alternate Ref.2
Modified residue2391N6-succinyllysine; alternate Ref.2
Modified residue2691N6-succinyllysine By similarity
Modified residue2961N6-acetyllysine; alternate By similarity
Modified residue2961N6-succinyllysine; alternate By similarity
Modified residue3011N6-acetyllysine; alternate By similarity
Modified residue3011N6-succinyllysine; alternate Ref.2
Modified residue3071N6-acetyllysine; alternate Ref.2
Modified residue3071N6-malonyllysine; alternate By similarity
Modified residue3071N6-succinyllysine; alternate By similarity
Modified residue3141N6-acetyllysine; alternate Ref.2
Modified residue3141N6-succinyllysine; alternate By similarity
Modified residue3241N6-acetyllysine; alternate By similarity
Modified residue3241N6-succinyllysine; alternate By similarity
Modified residue3281N6-acetyllysine; alternate Ref.2
Modified residue3281N6-succinyllysine; alternate Ref.2
Modified residue3291N6-acetyllysine; alternate By similarity
Modified residue3291N6-malonyllysine; alternate Ref.2
Modified residue3351N6-acetyllysine; alternate By similarity
Modified residue3351N6-succinyllysine; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q32LG3 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 575B305752E11569

FASTA33835,668
        10         20         30         40         50         60 
MLSALARPAG AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV SRLTLYDIAH 

        70         80         90        100        110        120 
TPGVAADLSH IETRATVKGY LGPEQLPDCL KGCDVVVIPA GVPRKPGMTR DDLFNTNATI 

       130        140        150        160        170        180 
VATLTAACAQ HCPEAMICII SNPVNSTIPI TAEVFKKHGV YNPNKIFGVT TLDIVRANAF 

       190        200        210        220        230        240 
VAELKDLDPA RVNVPVIGGH AGKTIIPLIS QCTPKVEFPQ DQLTTLTGRI QEAGTEVVKA 

       250        260        270        280        290        300 
KAGAGSATLS MAYAGARFVF SLVDAMNGKE GVVECSFVKS QETDCPYFST PLLLGKKGIE 

       310        320        330 
KNLGIGKVSP FEEKMIAEAI PELKASIKKG EEFVKNMK 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Liver.
[2]"Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase."
Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J., Hao Q., Lin H.
Science 334:806-809(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-185; LYS-307; LYS-314 AND LYS-328, MALONYLATION AT LYS-239 AND LYS-329, SUCCINYLATION AT LYS-239; LYS-301 AND LYS-328.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC109597 mRNA. Translation: AAI09598.1.
RefSeqXP_005225065.1. XM_005225008.1.
UniGeneBt.7915.

3D structure databases

ProteinModelPortalQ32LG3.
SMRQ32LG3. Positions 25-337.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ32LG3. 1 interaction.
STRING9913.ENSBTAP00000041906.

Proteomic databases

PaxDbQ32LG3.
PRIDEQ32LG3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281306.
KEGGbta:281306.

Organism-specific databases

CTD4191.

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213792.
HOVERGENHBG001662.
InParanoidQ32LG3.
KOK00026.

Enzyme and pathway databases

SABIO-RKQ32LG3.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR010097. Malate_DH_type1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11540. PTHR11540. 1 hit.
PTHR11540:SF1. PTHR11540:SF1. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDHM_BOVIN
AccessionPrimary (citable) accession number: Q32LG3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: December 6, 2005
Last modified: March 19, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families