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Q84FY8 (MDH_METEA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. 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:MexAM1_META1p1537
OrganismMethylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1) [Complete proteome] [HAMAP]
Taxonomic identifier272630 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

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_0000113457

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

Experimental info

Sequence conflict1091E → K in AAO24626. Ref.1
Sequence conflict1201T → A in AAO24626. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q84FY8 [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: B2CF23AAA0F032EC

FASTA32033,647
        10         20         30         40         50         60 
MARSKIALIG AGQIGGTLAH LAGLKELGDV VLFDIVDGVP QGKALDIAES APVDGFDAKY 

        70         80         90        100        110        120 
SGASDYSAIA GADVVIVTAG VPRKPGMSRD DLIGINLKVM EAVGAGIKEH APDAFVICIT 

       130        140        150        160        170        180 
NPLDAMVWAL QKFSGLPTNK VVGMAGVLDS ARFRHFLAEE FGVSVEDVTA FVLGGHGDDM 

       190        200        210        220        230        240 
VPLTRYSTVA GVPLTDLVKL GWTTQEKLDA MVERTRKGGG EIVNLLKTGS AFYAPAASAI 

       250        260        270        280        290        300 
AMAESYLRDK KRVLPCAAYL DGQYGIDGLY VGVPVVIGEN GVERVLEVTF NDDEKAMFEK 

       310        320 
SVNSVKGLIE ACKSVNDKLA 

« Hide

References

« Hide 'large scale' references
[1]"Methylotrophy in Methylobacterium extorquens AM1 from a genomic point of view."
Chistoserdova L., Chen S.-W., Lapidus A., Lidstrom M.E.
J. Bacteriol. 185:2980-2987(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Methylobacterium genome sequences: a reference blueprint to investigate microbial metabolism of C1 compounds from natural and industrial sources."
Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E. expand/collapse author list , Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C., Lidstrom M.E.
PLoS ONE 4:E5584-E5584(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14718 / DSM 1338 / AM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY181040 Genomic DNA. Translation: AAO24626.1.
CP001510 Genomic DNA. Translation: ACS39399.1.
RefSeqYP_002962676.1. NC_012808.1.

3D structure databases

ProteinModelPortalQ84FY8.
SMRQ84FY8. Positions 1-314.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ84FY8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS39399; ACS39399; MexAM1_META1p1537.
GeneID7991516.
KEGGmea:Mex_1p1537.
PATRIC22508920. VBIMetExt101010_1536.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAYAPSAFV.
OrthoDBEOG6091FG.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-4226.
MEXT272630:GBY6-1477-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_METEA
AccessionPrimary (citable) accession number: Q84FY8
Secondary accession number(s): C5B049
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: September 22, 2009
Last modified: May 14, 2014
This is version 72 of the entry and version 2 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