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B0SF41 (MDH_LEPBA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:LBF_1102
OrganismLeptospira biflexa serovar Patoc (strain Patoc 1 / Ames) [Complete proteome] [HAMAP]
Taxonomic identifier355278 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length327 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 – 327327Malate dehydrogenase HAMAP-Rule MF_01517
PRO_1000191623

Regions

Nucleotide binding11 – 177NAD By similarity
Nucleotide binding129 – 1313NAD By similarity

Sites

Active site1871Proton acceptor By similarity
Binding site921Substrate By similarity
Binding site981Substrate By similarity
Binding site1051NAD By similarity
Binding site1121NAD By similarity
Binding site1311Substrate By similarity
Binding site1621Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B0SF41 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: A0CE4ACD82D54BE4

FASTA32734,931
        10         20         30         40         50         60 
MSKKVKVAVT GAAGQIGYAL LFRIASGQMF GPDTAVELQL LELEQAIPAA KGVIMELDDC 

        70         80         90        100        110        120 
AFPLLEKVSV SSNIDEAFRD INWALLVGSV PRKAGMERGD LLKINGGIFT TQGKAIEKNA 

       130        140        150        160        170        180 
ASDVRVLVVG NPCNTNALIA MNNAKGVPSD RWFAMTGLDE NRAKTQLAQK AGVLVKDVSN 

       190        200        210        220        230        240 
VAIWGNHSAT QYPDFFNAKV NGKPATDVIS DHDWLKGDFI STVQKRGAAI IAARGASSAA 

       250        260        270        280        290        300 
SAANAVVDTV HNIVTPTKPG DWFSAACHSN GEYGVDKGLI FGYPLKSDGK KVEIVTGLEI 

       310        320 
NAFGKEKFDI THNELKEERN EVKDMLG 

« Hide

References

[1]"Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A. expand/collapse author list , Davies J.K., Medigue C., Adler B.
PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Patoc 1 / Ames.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000777 Genomic DNA. Translation: ABZ93628.1.
RefSeqYP_001962206.1. NC_010842.1.

3D structure databases

ProteinModelPortalB0SF41.
SMRB0SF41. Positions 3-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING355278.LBF_1102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ93628; ABZ93628; LBF_1102.
GeneID6388414.
KEGGlbf:LBF_1102.
PATRIC22341205. VBILepBif95142_1171.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMAWLENIMI.
OrthoDBEOG6PP9Q2.

Enzyme and pathway databases

BioCycLBIF355278:GHTJ-1101-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_LEPBA
AccessionPrimary (citable) accession number: B0SF41
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 50 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