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Q5X2T6 (MDH_LEGPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. 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:lpp2301
OrganismLegionella pneumophila (strain Paris) [Complete proteome] [HAMAP]
Taxonomic identifier297246 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_01517

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_01517

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01517

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 2 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 – 330330Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000113371

Regions

Nucleotide binding12 – 187NAD By similarity
Nucleotide binding130 – 1323NAD By similarity

Sites

Active site1881Proton acceptor By similarity
Binding site931Substrate By similarity
Binding site991Substrate By similarity
Binding site1061NAD By similarity
Binding site1131NAD By similarity
Binding site1321Substrate By similarity
Binding site1631Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5X2T6 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 3C36348E4E1BCAEA

FASTA33036,007
        10         20         30         40         50         60 
MTNNRVRVAV TGAAGQIGYA LVFRIASGQM FGPNTEVELN LLELEPALPS LEGVAMELDD 

        70         80         90        100        110        120 
CAFPLLKRIV CTADLNKAMD GVNWALLVGS VPRKQGMERS DLLQINGGIF TKQGQAINDY 

       130        140        150        160        170        180 
ASDDVRVFVV GNPCNTNCLI AMNHAKDVPS DRFYAMTTLD ELRARTQLAK KAGVDITAVT 

       190        200        210        220        230        240 
QMTIWGNHSA TQYPDFYNAK INGTSAAQVI NDETWLKETF VSTVQQRGAA VIKARGSSSA 

       250        260        270        280        290        300 
ASAANAIITG VNHLVTDTPA GESFSMCRRS KGEYGVDEGL IFSFPCRREH GELKVVENLE 

       310        320        330 
FNDFGRERFN TTLNELRSER DTVKSLGLLD 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Paris.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628336 Genomic DNA. Translation: CAH13454.1.
RefSeqYP_124612.1. NC_006368.1.

3D structure databases

ProteinModelPortalQ5X2T6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297246.lpp2301.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH13454; CAH13454; lpp2301.
GeneID3119651.
KEGGlpp:lpp2301.
PATRIC22325171. VBILegPne27771_2624.

Organism-specific databases

LegioListlpp2301.
CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMAAFSQECI.
OrthoDBEOG6PP9Q2.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_01517. Malate_dehydrog_2.
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.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR23382. PTHR23382. 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.
TIGRFAMsTIGR01759. MalateDH-SF1. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_LEGPA
AccessionPrimary (citable) accession number: Q5X2T6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 68 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