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Q2YAQ4 (MDH_NITMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:Nmul_A0864
OrganismNitrosospira multiformis (strain ATCC 25196 / NCIMB 11849) [Complete proteome] [HAMAP]
Taxonomic identifier323848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosospira

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_0000294396

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
Q2YAQ4 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: C0389CE276C78698

FASTA32735,521
        10         20         30         40         50         60 
MKTPIRVAVT GAAGQIAYSL LFRIAAGDML GEDQPVILQL LDIPQSLPSL KGVVMELDDC 

        70         80         90        100        110        120 
AFPLLRDITI TDDPKTAFRD INIAMLVGAR PRTKGMERKD LLEANGTIFR AQGKALDEVA 

       130        140        150        160        170        180 
GRDVKVLVVG NPANTNAYIT MKNAPSLKPT SFSSMMRLDH NRAVFQLAVK VGQPVSSVRK 

       190        200        210        220        230        240 
MIVWGNHSSA QYPDLSHAEV DGHNAADLVN DMAWIETGFI PVIQKRGMEV IEARGSSSAA 

       250        260        270        280        290        300 
SAANAAICHM RDWVSGTPEG DWVSMGIPSD GSYGIPEGVI YGYPVTCQGG EYKIVPDLEI 

       310        320 
SEFSRMKMQA SYRELMGERE SIKHLLG 

« Hide

References

[1]"Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC 25196."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25196 / NCIMB 11849.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000103 Genomic DNA. Translation: ABB74167.1.
RefSeqYP_411559.1. NC_007614.1.

3D structure databases

ProteinModelPortalQ2YAQ4.
SMRQ2YAQ4. Positions 1-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323848.Nmul_A0864.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB74167; ABB74167; Nmul_A0864.
GeneID3784434.
KEGGnmu:Nmul_A0864.
PATRIC22724872. VBINitMul110821_1007.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycNMUL323848:GKEC-885-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_NITMU
AccessionPrimary (citable) accession number: Q2YAQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: December 20, 2005
Last modified: February 19, 2014
This is version 60 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