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Q0AFK6 (MDH_NITEC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Malate dehydrogenase
EC=1.1.1.37
Gene names
Name:mdh
Ordered Locus Names:Neut_1633
OrganismNitrosomonas eutropha (strain C91) [Complete proteome] [HAMAP]
Taxonomic identifier335283 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Nitrosomonadales › Nitrosomonadaceae › Nitrosomonas ›

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: HAMAP

   Molecular_functionL-malate dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000294395

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
Q0AFK6 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 61F13E5BAEEA1567

FASTA32736,103
        10         20         30         40         50         60 
MLSPVRITVT GAAGQISYSL LFRIAAGDML GSNQPVILQL LDIPESRKIL DGVVMELQDC 

        70         80         90        100        110        120 
AFPLLAGIIA THDPMMAFDQ TDIAILVGAR PRRKGMERKD LLQTNGEIFR NQGKILNQVA 

       130        140        150        160        170        180 
KRDAKILVVG NPANTNTLIT MKNAPDLPAE NFSGMLRLDH NRALSQVAMK LNQPVSNIKK 

       190        200        210        220        230        240 
MIVWGNHSST QFPDLYHAEI GDTKVINLIK DPIWIENYFI PTVQKRGAVV IEARGLSSAA 

       250        260        270        280        290        300 
SAANAIIDHL RNWFFGTADG DWTTMGILSD GSYEIPEGVI YGFPVICKNG MREIVQGLEI 

       310        320 
NPFSRTRLDA AYNELTQELD SIRHLLP

« Hide

References

[1]"Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas eutropha C91: implications for niche adaptation."
Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.
Environ. Microbiol. 9:2993-3007(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C91.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000450 Genomic DNA. Translation: ABI59876.1.
RefSeqYP_747841.1. NC_008344.1.

3D structure databases

ProteinModelPortalQ0AFK6.
SMRQ0AFK6. Positions 6-325.
ModBaseSearch...

Protein-protein interaction databases

STRING335283.Neut_1633.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI59876; ABI59876; Neut_1633.
GeneID4272497.
KEGGnet:Neut_1633.
PATRIC22720698. VBINitEut7577_2002.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMANCLIASK.
ProtClustDBPRK05442.

Enzyme and pathway databases

BioCycNEUT335283:GHT6-1666-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. Lactate_DH/Glyco_hydro_4_C. 1 hit.
TIGRFAMsTIGR01759. MalateDH-SF1. 1 hit.
PROSITEPS00068. MDH. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_NITEC
AccessionPrimary (citable) accession number: Q0AFK6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: October 17, 2006
Last modified: May 29, 2013
This is version 51 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

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