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Q5NYA9 (MDH_AROAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. 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:AZOSEA38300
ORF Names:ebA6695
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum

Protein attributes

Sequence length329 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 – 329329Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000113347

Regions

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

Sites

Active site1911Proton acceptor By similarity
Binding site931Substrate By similarity
Binding site991Substrate By similarity
Binding site1061NAD By similarity
Binding site1131NAD By similarity
Binding site1321Substrate By similarity
Binding site1661Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5NYA9 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 69EF1CBDC1B3003F

FASTA32935,032
        10         20         30         40         50         60 
MSKAPVRVAV TGAAGQIGYS LLFRIASGEM LGKDQPVILQ LLDLPQAQKA VKGVMMELED 

        70         80         90        100        110        120 
CAFPLLAGMV ATDDPNVAFK DADYCLLVGA RPRGPGMERA DLLTANGAIF TVQGKAIAEN 

       130        140        150        160        170        180 
ANENVKVLVV GNPCNTNAYI AGAAARKVGR TNPNNYHGML RLDHNRALSQ LAAKTGRPVS 

       190        200        210        220        230        240 
SLKKMVVWGN HSPTMYADYR FCTSNGDSVK ALVNDHAWNN DVFLPTVGKR GAAIIDARGL 

       250        260        270        280        290        300 
SSAASAANAA IDHMHDWALG SDDWVTMGVP SDGSYGIPAG VVFGVPCECK NGDFKIIQGL 

       310        320 
EIDEYSREKI NKTLGELEDE RAAVADMLK 

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR555306 Genomic DNA. Translation: CAI09955.1.
RefSeqYP_160856.1. NC_006513.1.

3D structure databases

ProteinModelPortalQ5NYA9.
SMRQ5NYA9. Positions 3-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING76114.ebA6695.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI09955; CAI09955; ebA6695.
GeneID3181211.
KEGGeba:ebA6695.
PATRIC20973871. VBIAroAro98752_3853.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMAIAPMIAR.
OrthoDBEOG6PP9Q2.

Enzyme and pathway databases

BioCycAARO76114:GJTA-3882-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_AROAE
AccessionPrimary (citable) accession number: Q5NYA9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 4, 2005
Last modified: May 14, 2014
This is version 72 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