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

B0CIT1 (MDH_BRUSI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:BSUIS_A1767
OrganismBrucella suis (strain ATCC 23445 / NCTC 10510) [Complete proteome] [HAMAP]
Taxonomic identifier470137 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 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 – 320320Malate dehydrogenase HAMAP-Rule MF_00487
PRO_1000081355

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

Sequences

Sequence LengthMass (Da)Tools
B0CIT1 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 0C7F5699F650E91B

FASTA32033,672
        10         20         30         40         50         60 
MARNKIALIG SGMIGGTLAH LAGLKELGDV VLFDIAEGTP QGKGLDIAES SPVDGFDAKF 

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

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

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

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

       310        320 
SVASVAGLCE ACIGIAPSLK 

« Hide

References

[1]"Brucella suis ATCC 23445 whole genome shotgun sequencing project."
Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M., Snyder E.E. expand/collapse author list , Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., Munk C., Brettin T.S.
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23445 / NCTC 10510.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000911 Genomic DNA. Translation: ABY38784.1.
RefSeqYP_001628354.1. NC_010169.1.

3D structure databases

ProteinModelPortalB0CIT1.
SMRB0CIT1. Positions 3-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING470137.BSUIS_A1767.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY38784; ABY38784; BSUIS_A1767.
GeneID5838246.
KEGGbmt:BSUIS_A1767.
PATRIC17871150. VBIBruSui83806_3355.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAGANSYEA.
OrthoDBEOG6091FG.
ProtClustDBPRK06223.

Enzyme and pathway databases

BioCycBSUI470137:GJIC-1758-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...

Entry information

Entry nameMDH_BRUSI
AccessionPrimary (citable) accession number: B0CIT1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: February 19, 2014
This is version 45 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