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B9MBP0 (MDH_ACIET) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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:Dtpsy_2281
OrganismAcidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)) [Complete proteome] [HAMAP]
Taxonomic identifier535289 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length328 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 – 328328Malate dehydrogenase HAMAP-Rule MF_01517
PRO_1000185082

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
B9MBP0 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 8B4416329D3787BB

FASTA32834,794
        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 AINDQAWNKD VFLPTVGKRG AAIIAARGLS 

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

       310        320 
AIDAFSQECI DKTLAELQGE QDGVKHLL 

« Hide

References

[1]"Complete sequence of Diaphorobacter sp. TPSY."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TPSY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001392 Genomic DNA. Translation: ACM33719.1.
RefSeqYP_002553719.1. NC_011992.1.

3D structure databases

ProteinModelPortalB9MBP0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING535289.Dtpsy_2281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM33719; ACM33719; Dtpsy_2281.
GeneID7384874.
KEGGdia:Dtpsy_2281.
PATRIC21781671. VBIDiaSp55748_2311.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMAAFSQECI.
OrthoDBEOG6PP9Q2.

Enzyme and pathway databases

BioCycAEBR535289:GHOO-2323-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_ACIET
AccessionPrimary (citable) accession number: B9MBP0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 40 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