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Q3BWU8 (MDH_XANC5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:XCV1034
OrganismXanthomonas campestris pv. vesicatoria (strain 85-10) [Complete proteome] [HAMAP]
Taxonomic identifier316273 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

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_0000294408

Regions

Nucleotide binding11 – 177NAD By similarity
Nucleotide binding131 – 1333NAD By similarity

Sites

Active site1891Proton acceptor By similarity
Binding site941Substrate By similarity
Binding site1001Substrate By similarity
Binding site1071NAD By similarity
Binding site1141NAD By similarity
Binding site1331Substrate By similarity
Binding site1641Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3BWU8 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 2EE4A79D7381A21A

FASTA32834,878
        10         20         30         40         50         60 
MKAPVRVAVT GAAGQIGYAL LFRIASGEML GKDQPVILQL LELPIEKAQA ALKGVMMELE 

        70         80         90        100        110        120 
DCAFPLLAGM VGTDDAEVAF KDVDIALLVG SRPRGPGMER KDLLLANAEI FTAQGAALNK 

       130        140        150        160        170        180 
VAKRDVKVLV VGNPANTNAY IAMKSAPDLD PKNFTAMLRL DHNRALSQLS AKLGKPVAGI 

       190        200        210        220        230        240 
EKLAVWGNHS PTMYPDYRFA TADGASVGDA INDQEWNAST FIPTVGKRGA AIIEARGLSS 

       250        260        270        280        290        300 
AASAANAAID HIRDWVLGTN GKWVTMGVPS DGSYGIPEGV MFGFPVTTEN GKYTIVKDLP 

       310        320 
IDDFSQKYID KTLAELEEER SGVAHLLG 

« Hide

References

[1]"Insights into genome plasticity and pathogenicity of the plant pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence."
Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., Niesbach-Kloesgen U. expand/collapse author list , Patschkowski T., Rueckert C., Rupp O., Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., Kaiser O.
J. Bacteriol. 187:7254-7266(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 85-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM039952 Genomic DNA. Translation: CAJ22665.1.
RefSeqYP_362765.1. NC_007508.1.

3D structure databases

ProteinModelPortalQ3BWU8.
SMRQ3BWU8. Positions 2-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316273.XCV1034.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ22665; CAJ22665; XCV1034.
GeneID3733584.
KEGGxcv:XCV1034.
PATRIC24091488. VBIXanCam71633_1251.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMANCLIASK.
OrthoDBEOG6PP9Q2.

Enzyme and pathway databases

BioCycXCAM316273:GJF8-1054-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_XANC5
AccessionPrimary (citable) accession number: Q3BWU8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: November 22, 2005
Last modified: May 14, 2014
This is version 62 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