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Q21VT3 (MDH2_ALBFT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 59. 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 2

EC=1.1.1.37
Gene names
Name:mdh2
Ordered Locus Names:Rfer_2403
OrganismAlbidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) (Rhodoferax ferrireducens) [Complete proteome] [HAMAP]
Taxonomic identifier338969 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeRhodoferax

Protein attributes

Sequence length334 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 – 334334Malate dehydrogenase 2 HAMAP-Rule MF_01517
PRO_0000294404

Regions

Nucleotide binding12 – 187NAD By similarity
Nucleotide binding130 – 1323NAD By similarity

Sites

Active site1911Proton acceptor By similarity
Binding site931Substrate By similarity
Binding site991Substrate By similarity
Binding site1061NAD By similarity
Binding site1131NAD By similarity
Binding site1321Substrate By similarity
Binding site1661Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q21VT3 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: ED1746FB0D5A4D6C

FASTA33435,806
        10         20         30         40         50         60 
MNQAPVRVTV TGAAGRVAYA LLFRIASGDM LGADQPVQLV LFDLPHAMKA MQGVVMELED 

        70         80         90        100        110        120 
CAFPLLTEII ATDDPVLAFS DTQIALLVSA RPRAVGAERL EVLADNAKIF AAQGAVIGRH 

       130        140        150        160        170        180 
ANPDCKVLVV GNPCNTNACV AMKAAQKFSR IPARNFAALL RLDHNRALAQ LALKTGRPVG 

       190        200        210        220        230        240 
GVKRLAVWGN HSPTVYADDR FTTIDGDSVP AIIDNIAWHH DTLVRTVDKR GEAILAARGL 

       250        260        270        280        290        300 
YAEASAASAA IDQMRDWWLG TRGEWTTMGV VSDGAYGVPA GLVFGFPVIT DCRDYRIVPG 

       310        320        330 
LAVDAFARGM IDVNVRELTA ELEIVKPLLP ELFG 

« Hide

References

[1]"Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., Richardson P.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-621 / DSM 15236 / T118.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000267 Genomic DNA. Translation: ABD70120.1.
RefSeqYP_523651.1. NC_007908.1.

3D structure databases

ProteinModelPortalQ21VT3.
SMRQ21VT3. Positions 4-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING338969.Rfer_2403.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD70120; ABD70120; Rfer_2403.
GeneID3962073.
KEGGrfr:Rfer_2403.
PATRIC23237495. VBIRhoFer131161_2751.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMAIDNIAWH.
OrthoDBEOG6091FG.

Enzyme and pathway databases

BioCycAFER338969:GHU9-2429-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 nameMDH2_ALBFT
AccessionPrimary (citable) accession number: Q21VT3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: April 18, 2006
Last modified: June 11, 2014
This is version 59 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