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O33525 (MDH_RHIL3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 96. 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:RL4439
OrganismRhizobium leguminosarum bv. viciae (strain 3841) [Complete proteome] [HAMAP]
Taxonomic identifier216596 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 – 320320Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113462

Regions

Nucleotide binding10 – 156NAD By similarity
Nucleotide binding119 – 1213NAD By similarity

Sites

Active site1761Proton acceptor By similarity
Binding site341NAD By similarity
Binding site831Substrate By similarity
Binding site891Substrate By similarity
Binding site961NAD By similarity
Binding site1211Substrate By similarity
Binding site1521Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O33525 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 2094407A42C2B1C8

FASTA32033,590
        10         20         30         40         50         60 
MARNKIALIG SGMIGGTLAH LAGLKELGDI VLFDIADGIP QGKGLDISQS SPVEGFDVNL 

        70         80         90        100        110        120 
TGASDYSAIE GADVCIVTAG VARKPGMSRD DLLGINLKVM EQVGAGIKKY APNAFVICIT 

       130        140        150        160        170        180 
NPLDAMVWAL QKFSGLPANK VVGMAGVLDS SRFRLFLAKE FNVSVQDVTA FVLGGHGDTM 

       190        200        210        220        230        240 
VPLARYSTVG GIPLTDLVTM GWVTKERLEE IIQRTRDGGA EIVGLLKTGS AYYAPAASAI 

       250        260        270        280        290        300 
EMAESYLKDK KRVLPCAAHL SGQYGVKDMY VGVPTVIGAG GVERIIEIDL NKTEKEAFDK 

       310        320 
SVGAVAGLCE ACINIAPALK 

« Hide

References

« Hide 'large scale' references
[1]Poole P.S., Allaway D., Smith M.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome of Rhizobium leguminosarum has recognizable core and accessory components."
Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F., Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H., East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I., Chillingworth T., Clarke K. expand/collapse author list , Cronin A., Davis P., Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.
Genome Biol. 7:R34.1-R34.20(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 3841.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ002750 Genomic DNA. Translation: CAA05717.1.
AM236080 Genomic DNA. Translation: CAK09925.1.
RefSeqYP_770009.1. NC_008380.1.

3D structure databases

ProteinModelPortalO33525.
SMRO33525. Positions 1-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216596.RL4439.

Proteomic databases

ProMEXO33525.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK09925; CAK09925; RL4439.
GeneID4402981.
KEGGrle:RL4439.
PATRIC23145749. VBIRhiLeg32091_5777.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAGANSYEA.
OrthoDBEOG6091FG.
ProtClustDBPRK06223.

Enzyme and pathway databases

BioCycRLEG216596:GKE5-4515-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.
TIGRFAMsTIGR01763. MalateDH_bact. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMDH_RHIL3
AccessionPrimary (citable) accession number: O33525
Secondary accession number(s): Q1MAW0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 96 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