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Q32LG3

- MDHM_BOVIN

UniProt

Q32LG3 - MDHM_BOVIN

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Protein

Malate dehydrogenase, mitochondrial

Gene
MDH2
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Enzyme regulationi

Enzyme activity is enhanced by acetylation By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571NAD By similarity
Binding sitei104 – 1041Substrate By similarity
Binding sitei110 – 1101Substrate By similarity
Binding sitei117 – 1171NAD By similarity
Binding sitei142 – 1421Substrate By similarity
Binding sitei176 – 1761Substrate By similarity
Active sitei200 – 2001Proton acceptor By similarity
Binding sitei251 – 2511NAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 377NAD By similarity
Nucleotide bindingi140 – 1423NAD By similarity

GO - Molecular functioni

  1. L-malate dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. internal protein amino acid acetylation Source: UniProtKB
  3. malate metabolic process Source: InterPro
  4. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

SABIO-RKQ32LG3.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, mitochondrial (EC:1.1.1.37)
Gene namesi
Name:MDH2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424Mitochondrion By similarityAdd
BLAST
Chaini25 – 338314Malate dehydrogenase, mitochondrialPRO_0000260267Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331O-linked (GlcNAc) By similarity
Modified residuei78 – 781N6-acetyllysine; alternate By similarity
Modified residuei78 – 781N6-succinyllysine; alternate By similarity
Modified residuei91 – 911N6-acetyllysine; alternate By similarity
Modified residuei91 – 911N6-succinyllysine; alternate By similarity
Modified residuei165 – 1651N6-acetyllysine By similarity
Modified residuei185 – 1851N6-acetyllysine; alternate1 Publication
Modified residuei185 – 1851N6-succinyllysine; alternate By similarity
Modified residuei203 – 2031N6-succinyllysine By similarity
Modified residuei215 – 2151N6-acetyllysine; alternate By similarity
Modified residuei215 – 2151N6-succinyllysine; alternate By similarity
Modified residuei239 – 2391N6-acetyllysine; alternate By similarity
Modified residuei239 – 2391N6-malonyllysine; alternate1 Publication
Modified residuei239 – 2391N6-succinyllysine; alternate1 Publication
Modified residuei269 – 2691N6-succinyllysine By similarity
Modified residuei296 – 2961N6-acetyllysine; alternate By similarity
Modified residuei296 – 2961N6-succinyllysine; alternate By similarity
Modified residuei301 – 3011N6-acetyllysine; alternate By similarity
Modified residuei301 – 3011N6-succinyllysine; alternate1 Publication
Modified residuei307 – 3071N6-acetyllysine; alternate1 Publication
Modified residuei307 – 3071N6-malonyllysine; alternate By similarity
Modified residuei307 – 3071N6-succinyllysine; alternate By similarity
Modified residuei314 – 3141N6-acetyllysine; alternate1 Publication
Modified residuei314 – 3141N6-succinyllysine; alternate By similarity
Modified residuei324 – 3241N6-acetyllysine; alternate By similarity
Modified residuei324 – 3241N6-succinyllysine; alternate By similarity
Modified residuei328 – 3281N6-acetyllysine; alternate1 Publication
Modified residuei328 – 3281N6-succinyllysine; alternate1 Publication
Modified residuei329 – 3291N6-acetyllysine; alternate By similarity
Modified residuei329 – 3291N6-malonyllysine; alternate1 Publication
Modified residuei335 – 3351N6-acetyllysine; alternate By similarity
Modified residuei335 – 3351N6-succinyllysine; alternate By similarity

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

PaxDbiQ32LG3.
PRIDEiQ32LG3.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

IntActiQ32LG3. 1 interaction.
STRINGi9913.ENSBTAP00000041906.

Structurei

3D structure databases

ProteinModelPortaliQ32LG3.
SMRiQ32LG3. Positions 25-337.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0039.
HOGENOMiHOG000213792.
HOVERGENiHBG001662.
InParanoidiQ32LG3.
KOiK00026.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProiIPR001557. 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]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q32LG3-1 [UniParc]FASTAAdd to Basket

« Hide

MLSALARPAG AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV    50
SRLTLYDIAH TPGVAADLSH IETRATVKGY LGPEQLPDCL KGCDVVVIPA 100
GVPRKPGMTR DDLFNTNATI VATLTAACAQ HCPEAMICII SNPVNSTIPI 150
TAEVFKKHGV YNPNKIFGVT TLDIVRANAF VAELKDLDPA RVNVPVIGGH 200
AGKTIIPLIS QCTPKVEFPQ DQLTTLTGRI QEAGTEVVKA KAGAGSATLS 250
MAYAGARFVF SLVDAMNGKE GVVECSFVKS QETDCPYFST PLLLGKKGIE 300
KNLGIGKVSP FEEKMIAEAI PELKASIKKG EEFVKNMK 338
Length:338
Mass (Da):35,668
Last modified:December 6, 2005 - v1
Checksum:i575B305752E11569
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC109597 mRNA. Translation: AAI09598.1.
RefSeqiXP_005225065.1. XM_005225008.1.
UniGeneiBt.7915.

Genome annotation databases

GeneIDi281306.
KEGGibta:281306.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC109597 mRNA. Translation: AAI09598.1 .
RefSeqi XP_005225065.1. XM_005225008.1.
UniGenei Bt.7915.

3D structure databases

ProteinModelPortali Q32LG3.
SMRi Q32LG3. Positions 25-337.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q32LG3. 1 interaction.
STRINGi 9913.ENSBTAP00000041906.

Proteomic databases

PaxDbi Q32LG3.
PRIDEi Q32LG3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 281306.
KEGGi bta:281306.

Organism-specific databases

CTDi 4191.

Phylogenomic databases

eggNOGi COG0039.
HOGENOMi HOG000213792.
HOVERGENi HBG001662.
InParanoidi Q32LG3.
KOi K00026.

Enzyme and pathway databases

SABIO-RK Q32LG3.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProi IPR001557. 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 ]
PANTHERi PTHR11540. PTHR11540. 1 hit.
Pfami PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMi SSF56327. SSF56327. 1 hit.
TIGRFAMsi TIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEi PS00068. MDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiMDHM_BOVIN
AccessioniPrimary (citable) accession number: Q32LG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: December 6, 2005
Last modified: September 3, 2014
This is version 72 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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