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P48364 (MDH_MORS5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. 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 5710)
Taxonomic identifier246794 [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.2

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 35 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_0000113316

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

Mutagenesis2291Q → H: Increases the thermal stability. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P48364 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 2C4A3253E5B5D2E6

FASTA31231,985
        10         20         30         40         50         60 
MKVAVLGAAG GIGQALALLL KTQLPAGSDL SLYDIAPVTP GVAVDLSHIP TDVTIAGFAG 

        70         80         90        100        110        120 
MDPTDALVGA DVVLISAGVA RKPGMDRSDL FNINAGIIKN LAGKCAEVCP NACIGIITNP 

       130        140        150        160        170        180 
VNTTVPIAAE VLKQAGVYDK RKLFGITTLD VIRSETFVSA LKGISLADVE VPVIGGHSGV 

       190        200        210        220        230        240 
TILPLLSQVK GVEFTAEEVV ALTARIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR 

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

       310 
ANITLGEEFV AG 

« Hide

References

[1]"Characterization of malate dehydrogenase from deep-sea psychrophilic Vibrio sp. strain no. 5710 and cloning of its gene."
Ohkuma M., Ohtoko K., Takada N., Hamamoto T., Usami R., Kudo T., Horikoshi K.
FEMS Microbiol. Lett. 137:247-252(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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: CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D78194 Genomic DNA. Translation: BAA11301.1.

3D structure databases

ProteinModelPortalP48364.
SMRP48364. Positions 1-310.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_MORS5
AccessionPrimary (citable) accession number: P48364
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 77 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