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P0C890 (MDH_PROVB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 29. 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
OrganismProsthecochloris vibrioformis (Chlorobium vibrioforme)
Taxonomic identifier1098 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeProsthecochloris

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Homotetramer; arranged as a dimer of dimers. Ref.2

Sequence similarities

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

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
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 – 310310Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113449

Regions

Nucleotide binding7 – 126NAD By similarity
Nucleotide binding117 – 1193NAD By similarity

Sites

Active site1741Proton acceptor By similarity
Binding site321NAD By similarity
Binding site811Substrate By similarity
Binding site871Substrate By similarity
Binding site941NAD By similarity
Binding site1191Substrate By similarity
Binding site1501Substrate By similarity

Secondary structure

......................................................... 310
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C890 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: DFF3033B27FEC714

FASTA31033,273
        10         20         30         40         50         60 
MKITVIGAGN VGATTAFRIA DKKLARELVL LDVVEGIPQG KGLDMYETGP VGLFDTKITG 

        70         80         90        100        110        120 
SNDYADTADS DIVIITAGLP RKPGMTREDL LMKNAGIVKE VTDNIMKHSK NPIIIVVSNP 

       130        140        150        160        170        180 
LDIMTHVAWV RSGLPKERVI GMAGVLDAAR FRSFIAMELG VSMQDINACV LGGHGDAMVP 

       190        200        210        220        230        240 
VVKYTTVAGI PISDLLPAET IDKLVERTRN GGAEIVEHLK QGSAFYSPGS SVVEMVESIV 

       250        260        270        280        290        300 
LDRKRVLPCA VGLEGQYGID KTFVGVPVKL GRNGVEQIYE INLDQADLDL LQKSAKIVDE 

       310 
NCKMLESTIG 

« Hide

References

[1]"Malate dehydrogenase from the mesophile Chlorobium vibrioforme and from the mild thermophile Chlorobium tepidum: molecular cloning, construction of a hybrid, and expression in Escherichia coli."
Naterstad K., Lauvrak V., Sirevag R.
J. Bacteriol. 178:7047-7052(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases."
Dalhus B., Saarinen M., Sauer U.H., Eklund P., Johansson K., Karlsson A., Ramaswamy S., Bjoerk A., Synstad B., Naterstad K., Sirevaag R., Eklund H.
J. Mol. Biol. 318:707-721(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80837 Genomic DNA. Translation: CAA56809.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GUZX-ray2.00A/B/C/D72-310[»]
1GV1X-ray2.50A/B/C/D1-310[»]
ProteinModelPortalP0C890.
SMRP0C890. Positions 1-305.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Other

EvolutionaryTraceP0C890.

Entry information

Entry nameMDH_PROVB
AccessionPrimary (citable) accession number: P0C890
Secondary accession number(s): P80038, P94687
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: October 14, 2008
Last modified: February 19, 2014
This is version 29 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