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Q1AWH4 (MDH_RUBXD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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:Rxyl_1290
OrganismRubrobacter xylanophilus (strain DSM 9941 / NBRC 16129) [Complete proteome] [HAMAP]
Taxonomic identifier266117 [NCBI]
Taxonomic lineageBacteriaActinobacteriaRubrobacteridaeRubrobacteralesRubrobacterineaeRubrobacteraceaeRubrobacter

Protein attributes

Sequence length325 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 – 325325Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000292375

Regions

Nucleotide binding9 – 157NAD By similarity
Nucleotide binding127 – 1293NAD By similarity

Sites

Active site1851Proton acceptor By similarity
Binding site901Substrate By similarity
Binding site961Substrate By similarity
Binding site1031NAD By similarity
Binding site1101NAD By similarity
Binding site1291Substrate By similarity
Binding site1601Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1AWH4 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: EE303E16E0FC0DCC

FASTA32535,044
        10         20         30         40         50         60 
MSKTVTVTGA AGAIGYAILF RIASGQMLGP DQKLRLKLLE IEPALKAAEG TAMELYDCAF 

        70         80         90        100        110        120 
PLLEAVDITA DPKEAFDGAN VCLLIGARPR QRGMERADLL EANGQIFKPQ GRAINDHAAD 

       130        140        150        160        170        180 
DVRVLVVGNP ANTNCLIAMN NAPDVPRERF SAMTRLDENR AVSMLAQKLG VGVEDVRDLV 

       190        200        210        220        230        240 
VWGNHSPTMF PDLFNARVKG QRAVDLVEME WYENEYIPRV GKRGAEIIEA RGASSAASAA 

       250        260        270        280        290        300 
NAAIDHVRDW MLGADSLHSM AVASSGQYGV EEGLVSSFPV RLPGGGEYEI PEGLEVGDFA 

       310        320 
RSKLEITIGE LKEERDAVRK LGLIG 

« Hide

References

[1]"Complete sequence of Rubrobacter xylanophilus DSM 9941."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 9941 / NBRC 16129.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000386 Genomic DNA. Translation: ABG04254.1.
RefSeqYP_644066.1. NC_008148.1.

3D structure databases

ProteinModelPortalQ1AWH4.
SMRQ1AWH4. Positions 5-324.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266117.Rxyl_1290.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG04254; ABG04254; Rxyl_1290.
GeneID4116953.
KEGGrxy:Rxyl_1290.
PATRIC23369438. VBIRubXyl52678_1324.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycRXYL266117:GH8O-1308-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.
IPR001252. Malate_DH_AS.
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.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_RUBXD
AccessionPrimary (citable) accession number: Q1AWH4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: July 11, 2006
Last modified: February 19, 2014
This is version 56 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