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Q3YS64 (MDH_EHRCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:Ecaj_0398
OrganismEhrlichia canis (strain Jake) [Complete proteome] [HAMAP]
Taxonomic identifier269484 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 – 313313Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000241947

Regions

Nucleotide binding11 – 166NAD By similarity
Nucleotide binding120 – 1223NAD By similarity

Sites

Active site1771Proton acceptor By similarity
Binding site351NAD By similarity
Binding site841Substrate By similarity
Binding site901Substrate By similarity
Binding site971NAD By similarity
Binding site1221Substrate By similarity
Binding site1531Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3YS64 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 8CF3E7B4C1836F23

FASTA31333,762
        10         20         30         40         50         60 
MIKRKKIALI GAGNIGGMIA YLIRLKNLGD VVLLDVNDGI AKGKALDMAE SSPVGKYNGE 

        70         80         90        100        110        120 
ILGTNNYADI EGADAIVVTA GITRKPGMSR EDLINTNVNI IKEVADNIGK YAPNAFVVVV 

       130        140        150        160        170        180 
TNPLDVMVFA MHKYSKLSSN MVVGMAGILD SARFSYFIAK ELNVSVDNVN SLVLGGHGDL 

       190        200        210        220        230        240 
MLPLVKYSSV AGISIADLIK IDLITQDKVD AIIERTRKGG EEIVSLLKIG SAYYAPAESA 

       250        260        270        280        290        300 
LLMIDSYLND RRLILPCSVY LKGEYGVSNL FVGVPVIIGR NGVEKIIELE LTEQEKNIFD 

       310 
NSVKLIKNLV SNV 

« Hide

References

[1]"The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies."
Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.
J. Bacteriol. 188:4015-4023(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Jake.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000107 Genomic DNA. Translation: AAZ68441.1.
RefSeqYP_303039.1. NC_007354.1.

3D structure databases

ProteinModelPortalQ3YS64.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269484.Ecaj_0398.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ68441; AAZ68441; Ecaj_0398.
GeneID3617612.
KEGGecn:Ecaj_0398.
PATRIC20574342. VBIEhrCan118076_0427.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAFVGVPVI.
OrthoDBEOG6091FG.
ProtClustDBPRK06223.

Enzyme and pathway databases

BioCycECAN269484:GI02-425-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_EHRCJ
AccessionPrimary (citable) accession number: Q3YS64
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: September 27, 2005
Last modified: February 19, 2014
This is version 65 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