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Q5L5E3 (MDH_CHLAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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:CAB701
OrganismChlamydophila abortus (strain DSM 27085 / S26/3) [Complete proteome] [HAMAP]
Taxonomic identifier218497 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

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_0000113355

Regions

Nucleotide binding15 – 217NAD By similarity
Nucleotide binding133 – 1353NAD By similarity

Sites

Active site1911Proton acceptor By similarity
Binding site961Substrate By similarity
Binding site1021Substrate By similarity
Binding site1091NAD By similarity
Binding site1161NAD By similarity
Binding site1351Substrate By similarity
Binding site1661Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5L5E3 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: 11209B9C49E7B1D3

FASTA33036,110
        10         20         30         40         50         60 
MVMKLTRTVS VAVTGGTGQI AYSFLFALAH GDVFGSDCGI DLRIYDLPGL ERVLSGVRME 

        70         80         90        100        110        120 
LDDGAYPLLQ SLRVTTSLED AFDGIDAAFL IGAAPRGPGM ERSDLLKRNG EIFSLQGSVL 

       130        140        150        160        170        180 
NTSAKRDAKI FVVGNPVNTN CWIAMSQAPR LNRRNFHSML RLDQNRMHTM LAHRAEVPLD 

       190        200        210        220        230        240 
EVSHVVIWGN HSAKQVPDFT QALISGKPAV EVIGDRDWLE NIMLPSIQNR GSAVIEARGK 

       250        260        270        280        290        300 
SSAASAARAL AEAARSIFLP KDGEWFSTGV CSDYNPYGIP EDLIFGFPCR MLPSGDYEIV 

       310        320        330 
PGLLWDTFIK NKIQISLDEI SQEKANVSLL 

« Hide

References

[1]"The Chlamydophila abortus genome sequence reveals an array of variable proteins that contribute to interspecies variation."
Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D., Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D., Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A., Price C., Barrell B.G., Parkhill J., Longbottom D.
Genome Res. 15:629-640(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 27085 / S26/3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR848038 Genomic DNA. Translation: CAH64148.1.
RefSeqYP_220099.1. NC_004552.2.

3D structure databases

ProteinModelPortalQ5L5E3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218497.CAB701.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH64148; CAH64148; CAB701.
GeneID3337606.
KEGGcab:CAB701.
PATRIC20202925. VBIChlAbo21869_0766.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMACRMLPSG.
OrthoDBEOG6PP9Q2.
ProtClustDBPRK05442.

Enzyme and pathway databases

BioCycCABO218497:GJB0-721-MONOMER.

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.
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.
ProtoNetSearch...

Entry information

Entry nameMDH_CHLAB
AccessionPrimary (citable) accession number: Q5L5E3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 21, 2005
Last modified: February 19, 2014
This is version 62 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