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A1W9K7 (MDH_ACISJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:Ajs_2791
OrganismAcidovorax sp. (strain JS42) [Complete proteome] [HAMAP]
Taxonomic identifier232721 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Sequence caution

The sequence ABM42932.1 differs from that shown. Reason: Erroneous initiation.

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

Initiator methionine11Removed By similarity
Chain2 – 328327Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000292367

Regions

Nucleotide binding12 – 187NAD By similarity
Nucleotide binding132 – 1343NAD By similarity

Sites

Active site1901Proton acceptor By similarity
Binding site951Substrate By similarity
Binding site1011Substrate By similarity
Binding site1081NAD By similarity
Binding site1151NAD By similarity
Binding site1341Substrate By similarity
Binding site1651Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1W9K7 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: A02967E44E7FA9BD

FASTA32834,838
        10         20         30         40         50         60 
MSKKPVRVAV TGAAGQIGYA LLFRIASGEM LGKDQPVILQ LLEIPDEKAQ NALKGVIMEL 

        70         80         90        100        110        120 
EDCAFPLLAG IEAHSDPMTA FKDTDYALLV GARPRGPGME RADLLAANAQ IFTAQGKALN 

       130        140        150        160        170        180 
AVASRNVKVL VVGNPANTNA YIAMKSAPDL PAKNFTAMLR LDHNRAASQL AAKGGFKVGD 

       190        200        210        220        230        240 
IKKLTVWGNH SPTMYADYRF ATVDGKSVKD AINDPAWYKD VFLPTVGKRG AAIIAARGLS 

       250        260        270        280        290        300 
SAASAANAAI DHMRDWALGS KGEWVTMGVP SNGEYGIPAG IVFGFPVTTE NGEYKIVEGL 

       310        320 
PIDAFSQECI DKTLAELQGE QDGVKHLL 

« Hide

References

[1]"Complete sequence of chromosome 1 of Acidovorax sp. JS42."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JS42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000539 Genomic DNA. Translation: ABM42932.1. Different initiation.
RefSeqYP_987008.1. NC_008782.1.

3D structure databases

ProteinModelPortalA1W9K7.
SMRA1W9K7. Positions 3-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING232721.Ajs_2791.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM42932; ABM42932; Ajs_2791.
GeneID4674373.
KEGGajs:Ajs_2791.
PATRIC20690937. VBIAciSp27161_2989.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OrthoDBEOG6PP9Q2.
ProtClustDBPRK05442.

Enzyme and pathway databases

BioCycASP232721:GHWE-2833-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_ACISJ
AccessionPrimary (citable) accession number: A1W9K7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: February 19, 2014
This is version 46 of the entry and version 2 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