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A4J5N8 (MDH_DESRM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:Dred_1867
OrganismDesulfotomaculum reducens (strain MI-1) [Complete proteome] [HAMAP]
Taxonomic identifier349161 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfotomaculum

Protein attributes

Sequence length308 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 – 308308Malate dehydrogenase HAMAP-Rule MF_00487
PRO_1000072418

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
A4J5N8 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 34F412B8F2B8A7F1

FASTA30833,015
        10         20         30         40         50         60 
MKRKKITIVG AGNVGATCAH WAAAKELGDI VLIDVAEGIP QGKALDLMEA APVEGYDSVI 

        70         80         90        100        110        120 
IGTNDYADTA DSDVVVITAG VARKPGMSRD DLLNINAGIV RKVTEEIVKY SPNAYLLIVT 

       130        140        150        160        170        180 
NPVDVSAYIA YKASGFSANR VFGLSGVLDS ARFRTFIARE LNVSFEDVIS FVLGGHGDDM 

       190        200        210        220        230        240 
VPMVRYTYVG GIPVEKLIPT DRLEAMVERA RKGGAEIVNY LKTGSAYYAP SASVMQMAEC 

       250        260        270        280        290        300 
ILKDKKRILP VSAFLQGEYG ESDVFSGVPA IIGGDGVEKI IELDLDDEEM AALRKSINSV 


RNNISKLG 

« Hide

References

[1]"Complete sequence of Desulfotomaculum reducens MI-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MI-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000612 Genomic DNA. Translation: ABO50391.1.
RefSeqYP_001113216.1. NC_009253.1.

3D structure databases

ProteinModelPortalA4J5N8.
SMRA4J5N8. Positions 1-307.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349161.Dred_1867.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO50391; ABO50391; Dred_1867.
GeneID4955588.
KEGGdrm:Dred_1867.
PATRIC21729955. VBIDesRed82656_2050.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycDRED349161:GHP6-1923-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_DESRM
AccessionPrimary (citable) accession number: A4J5N8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 1, 2007
Last modified: February 19, 2014
This is version 51 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