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P10584 (MDH_THETH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

EC=1.1.1.37
Gene names
Name:mdh
OrganismThermus thermophilus
Taxonomic identifier274 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate. HAMAP-Rule MF_01517

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_01517

Subunit structure

Homodimer.

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 2 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000113400

Regions

Nucleotide binding11 – 177NAD HAMAP-Rule MF_01517
Nucleotide binding129 – 1313NAD HAMAP-Rule MF_01517

Sites

Active site1871Proton acceptor By similarity
Binding site921Substrate By similarity
Binding site981Substrate By similarity
Binding site1051NAD
Binding site1121NAD
Binding site1311Substrate By similarity
Binding site1621Substrate By similarity

Natural variations

Natural variant1901T → I in strain: F428; produces a 2 to 3 times higher enzyme activity.

Secondary structure

....................................................... 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10584 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 31FA90DED2393DF2

FASTA32735,426
        10         20         30         40         50         60 
MKAPVRVAVT GAAGQIGYSL LFRIAAGEML GKDQPVILQL LEIPQAMKAL EGVVMELEDC 

        70         80         90        100        110        120 
AFPLLAGLEA TDDPKVAFKD ADYALLVGAA PRKAGMERRD LLQVNGKIFT EQGRALAEVA 

       130        140        150        160        170        180 
KKDVKVLVVG NPANTNALIA YKNAPGLNPR NFTAMTRLDH NRAKAQLAKK TGTGVDRIRR 

       190        200        210        220        230        240 
MTVWGNHSST MFPDLFHAEV DGRPALELVD MEWYEKVFIP TVAQRGAAII QARGASSAAS 

       250        260        270        280        290        300 
AANAAIEHIR DWALGTPEGD WVSMAVPSQG EYGIPEGIVY SFPVTAKDGA YRVVEGLEIN 

       310        320 
EFARKRMEIT AQELLDEMEQ VKALGLI 

« Hide

References

[1]"Nucleotide sequence of the malate dehydrogenase gene of Thermus flavus and its mutation directing an increase in enzyme activity."
Nishiyama M., Matsubara N., Yamamoto K., Iijima S., Uozumi T., Beppu T.
J. Biol. Chem. 261:14178-14183(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-37 AND 265-284.
Strain: ATCC 33923 / DSM 674 / AT-62.
[2]"Characterization of an operon encoding succinyl-CoA synthetase and malate dehydrogenase from Thermus flavus AT-62 and its expression in Escherichia coli."
Nishiyama M., Horinouchi S., Beppu T.
Mol. Gen. Genet. 226:1-9(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 33923 / DSM 674 / AT-62.
[3]"Cloning and nucleotide sequences of the mdh and sucD genes from Thermus aquaticus B."
Nicholls D.J., Sundaram T.K., Atkinson T., Minton N.P.
FEMS Microbiol. Lett. 58:7-14(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: B / NCIB 11247.
[4]"Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus."
Kelly C.A., Nishiyama M., Ohnishi Y., Beppu T., Birktoft J.J.
Biochemistry 32:3913-3922(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Strain: ATCC 33923 / DSM 674 / AT-62.
[5]"Crystal structure of NAD-dependent malate dehydrogenase complexed with NADP(H)."
Tomita T., Fushinobu S., Kuzuyama T., Nishiyama M.
Biochem. Biophys. Res. Commun. 334:613-618(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH NADP.
[6]"Crystal structure of malate dehydrogenase from Thermus thermophilus HB8."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2002) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02598 Genomic DNA. Translation: AAA27499.1.
X54073 Genomic DNA. Translation: CAA38008.1.
X56033 Genomic DNA. Translation: CAA39508.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BDMX-ray1.80A/B1-327[»]
1BMDX-ray1.90A/B1-327[»]
1IZ9X-ray2.00A/B1-327[»]
1WZEX-ray2.00A/B1-327[»]
1WZIX-ray2.00A/B1-327[»]
1Y7TX-ray1.65A/B1-327[»]
2CVQX-ray2.08A/B1-321[»]
4KDEX-ray1.80A/B1-327[»]
4KDFX-ray2.36A/B/C/D1-327[»]
ProteinModelPortalP10584.
SMRP10584. Positions 1-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262724.TTC0168.

Chemistry

BindingDBP10584.
ChEMBLCHEMBL4255.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP10584.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_01517. Malate_dehydrog_2.
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.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR23382. PTHR23382. 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.
TIGRFAMsTIGR01759. MalateDH-SF1. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10584.

Entry information

Entry nameMDH_THETH
AccessionPrimary (citable) accession number: P10584
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references