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Q9HJL5 (MDH_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 93. 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:Ta0952
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length325 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
Reference 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 – 325325Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113495

Regions

Nucleotide binding10 – 156NAD By similarity
Nucleotide binding124 – 1263NAD By similarity

Sites

Active site1811Proton acceptor By similarity
Binding site341NAD By similarity
Binding site881Substrate By similarity
Binding site941Substrate By similarity
Binding site1011NAD By similarity
Binding site1261Substrate By similarity
Binding site1571Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HJL5 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: D6126D95B7EB1B31

FASTA32535,524
        10         20         30         40         50         60 
MARKKISVIG AGNVGATVAQ FLAAKQLGDV YLFDVVDGIP EGKALDIQEG APHWRYDLDV 

        70         80         90        100        110        120 
VGFSTSDETK YKNMEGSDVI VVTAGLARKP GMSRDDLFDK NVEIISDVSR NIKKYSPDSI 

       130        140        150        160        170        180 
IVVVSNPADI MAYALQKFTG IDPSKIMGLG GSLDSSRFRT FLAKELNVSV EDVNAFVIGG 

       190        200        210        220        230        240 
HGDDMVPFIR YSSVAGIPIE NLLSKEKIDE IVKRTRFGGG EIVNYLKTGS AFYAPGISIT 

       250        260        270        280        290        300 
AMVESVIMDK KRVIPCAAYI TGKHADHYGI RDKFIGVPIK IGEKGVEQIY DIDFKPDELE 

       310        320 
LWKKSVASVE ASSKKVDEWI AKHAH 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of the gene for the L-malate dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum."
Martinez D., Trejo F., Gelpi J.L., Busquets M., Cortes A.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF199510 Genomic DNA. Translation: AAG28562.1.
AL445066 Genomic DNA. Translation: CAC12081.1.
RefSeqNP_394412.1. NC_002578.1.

3D structure databases

ProteinModelPortalQ9HJL5.
SMRQ9HJL5. Positions 5-312.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273075.Ta0952.

Proteomic databases

PRIDEQ9HJL5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC12081; CAC12081; CAC12081.
GeneID1456484.
KEGGtac:Ta0952.

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAGANSYEA.
ProtClustDBPRK06223.

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.
TIGRFAMsTIGR01763. MalateDH_bact. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMDH_THEAC
AccessionPrimary (citable) accession number: Q9HJL5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: March 1, 2001
Last modified: February 19, 2014
This is version 93 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