Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q1IWC9 (MDH_DEIGD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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
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:Dgeo_2161
OrganismDeinococcus geothermalis (strain DSM 11300) [Complete proteome] [HAMAP]
Taxonomic identifier319795 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

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 MF_01517

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP MF_01517

Subunit structure

Homodimer By similarity. HAMAP MF_01517

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 334334Malate dehydrogenase HAMAP MF_01517
PRO_0000292372

Regions

Nucleotide binding17 – 237NAD By similarity
Nucleotide binding135 – 1373NAD By similarity

Sites

Active site1931Proton acceptor By similarity
Binding site981Substrate By similarity
Binding site1041Substrate By similarity
Binding site1111NAD By similarity
Binding site1181NAD By similarity
Binding site1371Substrate By similarity
Binding site1681Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1IWC9 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: E011483F19313371

FASTA33435,928
        10         20         30         40         50         60 
MTMNQGTKQP VRVAVTGAAG QIGYSLLFRI AAGDMLGKDQ PVILQLLEIT PALKALAGVV 

        70         80         90        100        110        120 
MELRDCAFPL LADIVTSDDP LVAFKDADYA LLVGAMPRKA GMERGDLLGA NGGIFKPQGE 

       130        140        150        160        170        180 
ALNKVASRDV KVLVVGNPAN TNALIAQQNA PDLDPKQFTA MVRLDHNRAI SQLAEKTGQP 

       190        200        210        220        230        240 
VSAIKNITIW GNHSSTQYPD LSQATVNGQP ALDLVDREWY EKEYIPTVAK RGAAIIEARG 

       250        260        270        280        290        300 
ASSAASAASA AIDHMRDWAL GTPEGEWVSM AVPSDGSYGI PEGLIYGFPV RCRNGQYEIV 

       310        320        330 
QGLEISDFSR QKMDATAKEL EEEREEVRRL GLVK

« Hide

References

[1]"Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300."
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., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 11300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000359 Genomic DNA. Translation: ABF46455.1.
RefSeqYP_605624.1. NC_008025.1.

3D structure databases

ProteinModelPortalQ1IWC9.
SMRQ1IWC9. Positions 8-333.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1IWC9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4058896.
GenomeReviewsGene locus Dgeo_2161 in contig CP000359_GR.
KEGGdge:Dgeo_2161.
NMPDRfig|68909.1.peg.1991.
PATRIC21626301. VBIDeiGeo41128_2761.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHBG289884.
OMADPNVAFK.
ProtClustDBPRK05442.

Enzyme and pathway databases

BioCycDGEO319795:DGEO_2161-MONOMER.

Family and domain databases

HAMAPMF_01517. Malate_dehydrog_2.
[Tree]
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]
Gene3DG3DSA:3.90.110.10. lact_mal_DH. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00024.
PANTHERPTHR23382. MDH_SF1. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMSSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
TIGRFAMsTIGR01759. MalateDH-SF1. 1 hit.
PROSITEPS00068. MDH. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_DEIGD
AccessionPrimary (citable) accession number: Q1IWC9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 13, 2006
Last modified: January 25, 2012
This is version 47 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents