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Q5HBC0 (MDH_EHRRW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:Erum4090, ERWE_CDS_04240
OrganismEhrlichia ruminantium (strain Welgevonden) [Complete proteome] [HAMAP]
Taxonomic identifier254945 [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.

Sequence caution

The sequence CAH58132.1 differs from that shown. Reason: Erroneous initiation.

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_0000241949

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
Q5HBC0 [UniParc].

Last modified June 27, 2006. Version 2.
Checksum: AE339233CEC06E2F

FASTA31333,729
        10         20         30         40         50         60 
MIQSKKIALI GSGNIGGMIA YLIRLKNLGD VVLLDINDGM AKGKALDIAE SSPIGKYNGE 

        70         80         90        100        110        120 
IFGTNNYADI ENADAIIVTA GITRKPGMSR DDLISTNVNI IKEIATNIAK YAPNAFVIVV 

       130        140        150        160        170        180 
TNPLDVMVLA MYRYSHLPSN MIVGMAGVLD SARFSYFIAK ELNVSVESVD SLVLGGHGDI 

       190        200        210        220        230        240 
MLPLIRYSSV SGVSIADLIK LGMITHDKVT EIVERTRKGG EEIVSLLKTG SAYYAPAESA 

       250        260        270        280        290        300 
VLMLDSYLND KKLMLPCSAY LKGEYGVHDL FVGVPIIIGK NGVEKIVELQ LTEEENSIFN 

       310 
NSVALIQNLV ANI 

« Hide

References

[1]"The genome of the heartwater agent Ehrlichia ruminantium contains multiple tandem repeats of actively variable copy number."
Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E., Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M., Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C., Berthier D., Botha M., Joubert F. expand/collapse author list , Corton C.H., Thomson N.R., Allsopp M.T., Allsopp B.A.
Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Welgevonden.
[2]"Comparative genomic analysis of three strains of Ehrlichia ruminantium reveals an active process of genome size plasticity."
Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.
J. Bacteriol. 188:2533-2542(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Welgevonden.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR767821 Genomic DNA. Translation: CAH58132.1. Different initiation.
CR925678 Genomic DNA. Translation: CAI26918.1.
RefSeqYP_180274.1. NC_005295.2.
YP_197300.1. NC_006832.1.

3D structure databases

ProteinModelPortalQ5HBC0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH58132; CAH58132; Erum4090.
CAI26918; CAI26918; ERWE_CDS_04240.
GeneID3233406.
3260940.
KEGGeru:Erum4090.
erw:ERWE_CDS_04240.
PATRIC20580669. VBIEhrRum92411_0450.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAFVINVAN.
OrthoDBEOG6091FG.

Enzyme and pathway databases

BioCycERUM254945:GJ2L-448-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_EHRRW
AccessionPrimary (citable) accession number: Q5HBC0
Secondary accession number(s): Q5FEX9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 27, 2006
Last modified: May 14, 2014
This is version 63 of the entry and version 2 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