Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B3E9R5 (MDH_GEOLS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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:Glov_1625
OrganismGeobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) [Complete proteome] [HAMAP]
Taxonomic identifier398767 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length321 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 – 321321Malate dehydrogenase HAMAP-Rule MF_00487
PRO_1000126134

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
B3E9R5 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 132CC17513E80EA6

FASTA32133,738
        10         20         30         40         50         60 
MGRKKISLIG GGQIGGVLAQ LCALRELGDV VMFDIVEGMP QGKMLDIAEA SPVDGFDVCL 

        70         80         90        100        110        120 
QGTQDYKDIA GSDVVIVTAG LPRKPGMSRD DLIATNSKIM TSVAEGIKQY ASNAFVIIIS 

       130        140        150        160        170        180 
NPLDAMVTLC QKITGMPANR VVGQAGVLDS ARFKAFIAWE LGVSVKDVSA MTLGGHGDDM 

       190        200        210        220        230        240 
VPLVRYAAVN GIPVMELLEQ KYGAEKAKEV MEAMVNRTRL AGGEVVALLK TGSAFYSPAS 

       250        260        270        280        290        300 
SAIAMAESVL KDQKRVLPTC CLLNGEFGVN GYYVGVPAVL GASGVEKILQ FKLDATEQAM 

       310        320 
MDKSVAAVKG LVDSLDSILK G 

« Hide

References

[1]"Complete sequence of chromosome of Geobacter lovleyi SZ."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E., Ritalahti K.M., Loeffler F.E., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1151 / DSM 17278 / SZ.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001089 Genomic DNA. Translation: ACD95341.1.
RefSeqYP_001951861.1. NC_010814.1.

3D structure databases

ProteinModelPortalB3E9R5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398767.Glov_1625.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD95341; ACD95341; Glov_1625.
GeneID6368374.
KEGGglo:Glov_1625.
PATRIC21994929. VBIGeoLov31523_1571.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMADLPQGKC.
OrthoDBEOG6091FG.
ProtClustDBPRK06223.

Enzyme and pathway databases

BioCycGLOV398767:GH32-1650-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_GEOLS
AccessionPrimary (citable) accession number: B3E9R5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 22, 2008
Last modified: February 19, 2014
This is version 42 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