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Q82WB9 (MDH_NITEU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. 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:NE0773
OrganismNitrosomonas europaea (strain ATCC 19718 / NBRC 14298) [Complete proteome] [HAMAP]
Taxonomic identifier228410 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length327 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 – 327327Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000113382

Regions

Nucleotide binding11 – 177NAD By similarity
Nucleotide binding129 – 1313NAD By similarity

Sites

Active site1871Proton acceptor By similarity
Binding site921Substrate By similarity
Binding site981Substrate By similarity
Binding site1051NAD By similarity
Binding site1121NAD By similarity
Binding site1311Substrate By similarity
Binding site1621Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82WB9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 3C8D52C94C8F740F

FASTA32736,000
        10         20         30         40         50         60 
MSSPIRIAVT GAAGQISYSL LFRIAAGDML GSSQPVILQL LDIPESGKVL DGVLMELQDC 

        70         80         90        100        110        120 
AFPLLTDIIV THDPMIAFDQ ADIAILVGAR PRGKGMERKD LLQTNGEIFR EQGRALNQVV 

       130        140        150        160        170        180 
KRDAKILVVG NPANTNTLIT MKNAPDLSPE NFSGMLRLDH NRALSQVAMK LNQPVSHIRK 

       190        200        210        220        230        240 
MIVWGNHSST QFPDLSHAEI DHQKVIDLIK DQTWVENSFI PTVQNRGAVV IEARGLSSAA 

       250        260        270        280        290        300 
SAANAIIDHM RDWIFGTRDD DWITMGILSD GSYKIPKGVI YGFPVVCKNG GRKIVQGLEI 

       310        320 
SPFSRTRLDI AYDELTQELD SIKHLLL 

« Hide

References

[1]"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea."
Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.
J. Bacteriol. 185:2759-2773(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19718 / NBRC 14298.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL954747 Genomic DNA. Translation: CAD84684.1.
RefSeqNP_840847.1. NC_004757.1.

3D structure databases

ProteinModelPortalQ82WB9.
SMRQ82WB9. Positions 1-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING228410.NE0773.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD84684; CAD84684; NE0773.
GeneID1081711.
KEGGneu:NE0773.
PATRIC22712522. VBINitEur56163_0865.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMADVHHCKV.
OrthoDBEOG6PP9Q2.
ProtClustDBPRK05442.

Enzyme and pathway databases

BioCycNEUR228410:GJNO-793-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_NITEU
AccessionPrimary (citable) accession number: Q82WB9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 77 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