Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2YLR9 (MDH_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BAB1_1927
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_00487

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_00487

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 3 family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete 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 – 320320Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000241943

Regions

Nucleotide binding10 – 156NAD By similarity
Nucleotide binding119 – 1213NAD By similarity

Sites

Active site1761Proton acceptor By similarity
Binding site341NAD By similarity
Binding site831Substrate By similarity
Binding site891Substrate By similarity
Binding site961NAD By similarity
Binding site1211Substrate By similarity
Binding site1521Substrate By similarity

Secondary structure

....................................................... 320
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q2YLR9 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: C212BA88F0241677

FASTA32033,704
        10         20         30         40         50         60 
MARNKIALIG SGMIGGTLAH LAGLKELGDV VLFDIAEGTP QGKGLDIAES SPVDGFDAKF 

        70         80         90        100        110        120 
TGANDYAAIE GADVVIVTAG VPRKPGMSRD DLLGINLKVM EQVGAGIKKY APEAFVICIT 

       130        140        150        160        170        180 
NPLDAMVWAL QKFSGLPAHK VVGMAGVLDS ARFRYFLSEE FNVSVEDVTV FVLGGHGDSM 

       190        200        210        220        230        240 
VPLARYSTVA GIPLPDLVKM GWTSQDKLDK IIQRTRDGGA EIVGLLKTGS AFYAPAASAI 

       250        260        270        280        290        300 
QMAESYLKDK KRVLPVAAQL SGQYGVKDMY VGVPTVIGAN GVERIIEIDL DKDEKAQFDK 

       310        320 
SVASVAGLCE ACIGIAPSLK 

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM040264 Genomic DNA. Translation: CAJ11883.1.
RefSeqYP_415266.1. NC_007618.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GVHX-ray2.30A/B/C/D1-320[»]
3GVIX-ray2.25A/B/C/D/E/F1-320[»]
ProteinModelPortalQ2YLR9.
SMRQ2YLR9. Positions 3-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING359391.BAB1_1927.

Proteomic databases

PRIDEQ2YLR9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ11883; CAJ11883; BAB1_1927.
GeneID3788794.
KEGGbmf:BAB1_1927.
PATRIC17846933. VBIBruMel86222_2007.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAYAPSAFV.
OrthoDBEOG6091FG.

Enzyme and pathway databases

BioCycBABO359391:GKDV-1978-MONOMER.
BMEL359391:GJOQ-1978-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_00487. Malate_dehydrog_3.
InterProIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR011275. Malate_DH_type3.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11540. PTHR11540. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSPR00086. LLDHDRGNASE.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01763. MalateDH_bact. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ2YLR9.

Entry information

Entry nameMDH_BRUA2
AccessionPrimary (citable) accession number: Q2YLR9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 20, 2005
Last modified: May 14, 2014
This is version 64 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names