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Q7X3X5 (MDH_MORS2) 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
OrganismMoritella sp. (strain 2D2)
Taxonomic identifier215801 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesMoritellaceaeMoritella

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate. HAMAP-Rule MF_01516

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. Ref.1

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01516

Sequence similarities

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

Biophysicochemical properties

pH dependence:

Optimum pH is 9.5-10.0 for malate dehydrogenation, and 7.5-8.0 for oxaloacetate reduction. HAMAP-Rule MF_01516

Temperature dependence:

Optimum temperature is 40 degrees Celsius.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandNAD
   Molecular functionOxidoreductase
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 – 312312Malate dehydrogenase HAMAP-Rule MF_01516
PRO_0000113315

Regions

Nucleotide binding7 – 137NAD By similarity
Nucleotide binding117 – 1193NAD By similarity

Sites

Active site1771Proton acceptor By similarity
Binding site341NAD By similarity
Binding site811Substrate By similarity
Binding site871Substrate By similarity
Binding site941NAD By similarity
Binding site1191Substrate By similarity
Binding site1531Substrate By similarity
Binding site2271NAD By similarity

Experimental info

Mutagenesis2291H → Q: Decreases the thermal stability. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q7X3X5 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: DA8A42A7C8F5DB1B

FASTA31231,941
        10         20         30         40         50         60 
MKVAVLGAAG GIGQALALLL KTQLPAGSEL SLYDIAPVTP GVAVDLSHIP TDVTITGFSG 

        70         80         90        100        110        120 
IDPTAALVGA DVVLISAGVA RKPGMDRSDL FNINAGIIKN LASKCAEVCP TACIGIITNP 

       130        140        150        160        170        180 
VNTTVPIAAE VLKQAGVYDK RKLFGITTLD VIRSETFVSA LKGISLADVA VPVIGGHSGA 

       190        200        210        220        230        240 
TILPLLSQVK GVEFTAEEIA TLTTRIQNAG TEVVEAKAGG GSATLSMGHA AARFGLSLVR 

       250        260        270        280        290        300 
ALQGEKGIVE CTYVDGGSEH ATFFAQPVLL GKNGVEEVLA YGDLSDFETN ARDAMLEELK 

       310 
ANITLGEEFV AG 

« Hide

References

[1]"Differences in malate dehydrogenases from the obligately piezophilic deep-sea bacterium Moritella sp. strain 2D2 and the psychrophilic bacterium Moritella sp. strain 5710."
Saito R., Nakayama A.
FEMS Microbiol. Lett. 233:165-172(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB097559 Genomic DNA. Translation: BAC77301.1.

3D structure databases

ProteinModelPortalQ7X3X5.
SMRQ7X3X5. Positions 1-310.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ7X3X5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.37. 7318.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_01516. Malate_dehydrog_1.
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.
IPR023958. Malate_DH_type1_bac.
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.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_MORS2
AccessionPrimary (citable) accession number: Q7X3X5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: October 1, 2003
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