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Q704B2 (MDH_THETK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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

EC=1.1.1.37
Gene names
Name:mdh
Ordered Locus Names:TTX_1427
OrganismThermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1) [Complete proteome] [HAMAP]
Taxonomic identifier768679 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaeThermoproteus

Protein attributes

Sequence length308 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_00487

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_00487

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 3 family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcellular carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

malate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionL-malate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 308308Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113496

Regions

Nucleotide binding6 – 116NAD By similarity
Nucleotide binding116 – 1183NAD By similarity

Sites

Active site1731Proton acceptor By similarity
Binding site311NAD By similarity
Binding site801Substrate By similarity
Binding site861Substrate By similarity
Binding site931NAD By similarity
Binding site1181Substrate By similarity
Binding site1491Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q704B2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6DB990BB5CFF19F2

FASTA30832,861
        10         20         30         40         50         60 
MITVVGSGRV GATTAAMLGV LGVDNKIVLI DIIKGLPQGE ALDLNHMSSI LGLDVYYTGS 

        70         80         90        100        110        120 
NDYADMKGSD LVIVTAGLAR KPGMTREQLL EQNAQIVANI GKEIAKYAPD SVVILTTNPL 

       130        140        150        160        170        180 
DAMTYVMWRA TGFSRERVVG FSGVLDGGRL AFYAGQKLGI SPASIIPIVL GQHGESMFPV 

       190        200        210        220        230        240 
PSKSFVFGVP LDKLLKPEEI KEAVEETVKA GARITELRGF SSNWAPGAGV AIMAKAVKRD 

       250        260        270        280        290        300 
ERRALIASVV LDGEYGVRGI PVEVPVVLGR GGAIKVLEVE LSPEEKQRFQ QSVEAISKLL 


NSLPAQYK 

« Hide

References

« Hide 'large scale' references
[1]"Reconstruction of the central carbohydrate metabolism of Thermoproteus tenax using genomic and biochemical data."
Siebers B., Tjaden B., Michalke K., Doerr C., Ahmed H., Zaparty M., Gordon P., Sensen C.W., Zibat A., Klenk H.-P., Schuster S.C., Hensel R.
J. Bacteriol. 186:2179-2194(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1.
[2]"The complete genome sequence of Thermoproteus tenax: a physiologically versatile member of the Crenarchaeota."
Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D., Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M., Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C., Hensel R.
PLoS ONE 6:E24222-E24222(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ621301 Genomic DNA. Translation: CAF18482.1.
FN869859 Genomic DNA. Translation: CCC82058.1.
RefSeqYP_004893136.1. NC_016070.1.

3D structure databases

ProteinModelPortalQ704B2.
SMRQ704B2. Positions 1-308.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCC82058; CCC82058; TTX_1427.
GeneID11262306.
KEGGttn:TTX_1427.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00024.
OMAGANSYEA.

Enzyme and pathway databases

BioCycTTEN768679:GJSY-1402-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_00487. Malate_dehydrog_3.
InterProIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR011275. Malate_DH_type3.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11540. PTHR11540. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSPR00086. LLDHDRGNASE.
SUPFAMSSF56327. SSF56327. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMDH_THETK
AccessionPrimary (citable) accession number: Q704B2
Secondary accession number(s): G4RKG3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 55 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