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Q07841 (MDH_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:rrnAC2706
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula

Protein attributes

Sequence length304 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate. HAMAP-Rule MF_00487

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_00487

Subunit structure

Homotetramer; arranged as a dimer of dimers. Ref.3 Ref.5 Ref.6

Subcellular location

Cytoplasm HAMAP-Rule MF_00487.

Miscellaneous

The quarternary structure is stabilized by chloride ions bound between the subunits. This may be an adaptation to the halophilic environment.

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 3 family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
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

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 304304Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113481

Regions

Nucleotide binding8 – 147NAD HAMAP-Rule MF_00487
Nucleotide binding119 – 1213NAD HAMAP-Rule MF_00487

Sites

Active site1761Proton acceptor By similarity
Binding site341NAD
Binding site831Substrate By similarity
Binding site891Substrate By similarity
Binding site961NAD
Binding site1211Substrate By similarity
Binding site1521Substrate By similarity

Experimental info

Mutagenesis831R → Q: Substrate specificity changes from oxaloacetate to pyruvate.
Sequence conflict191Y → T AA sequence Ref.1

Secondary structure

.................................................... 304
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07841 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 0B5B630158CAD083

FASTA30432,808
        10         20         30         40         50         60 
MTKVSVVGAA GTVGAAAGYN IALRDIADEV VFVDIPDKED DTVGQAADTN HGIAYDSNTR 

        70         80         90        100        110        120 
VRQGGYEDTA GSDVVVITAG IPRQPGQTRI DLAGDNAPIM EDIQSSLDEH NDDYISLTTS 

       130        140        150        160        170        180 
NPVDLLNRHL YEAGDRSREQ VIGFGGRLDS ARFRYVLSEE FDAPVQNVEG TILGEHGDAQ 

       190        200        210        220        230        240 
VPVFSKVRVD GTDPEFSGDE KEQLLGDLQE SAMDVIERKG ATEWGPARGV AHMVEAILHD 

       250        260        270        280        290        300 
TGEVLPASVK LEGEFGHEDT AFGVPVRLGS NGVEEIVEWD LDDYEQDLMA DAAEKLSDQY 


DKIS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui."
Cendrin F., Chroboczek J., Zaccai G., Eisenberg H., Mevarech M.
Biochemistry 32:4308-4313(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-55.
[2]"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea."
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V.
Genome Res. 14:2221-2234(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[3]"Insights into the molecular relationships between malate and lactate dehydrogenases: structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric L-[LDH-like] malate dehydrogenase from the halophilic archaeon Haloarcula marismortui."
Madern D., Ebel C., Mevarech M., Richard S.B., Pfister C., Zaccai G.
Biochemistry 39:1001-1010(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[4]"Structural features that stabilize halophilic malate-dehydrogenase from an archaebacterium."
Dym O., Mevarech M., Sussman J.L.
Science 267:1344-1346(1995)
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
[5]"Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 A resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui."
Richard S.B., Madern D., Garcin E., Zaccai G.
Biochemistry 39:992-1000(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS), SUBUNIT.
[6]"The oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies."
Irimia A., Ebel C., Madern D., Richard S.B., Cosenza L.W., Zaccai G., Vellieux F.M.D.
J. Mol. Biol. 326:859-873(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97218 Genomic DNA. Translation: AAA73368.1.
AY596297 Genomic DNA. Translation: AAV47474.1.
PIRA49496.
RefSeqYP_137180.1. NC_006396.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D3AX-ray2.94A/B2-304[»]
1HLPX-ray3.20A/B2-304[»]
1O6ZX-ray1.95A/B/C/D2-304[»]
2HLPX-ray2.59A/B2-304[»]
2J5KX-ray2.00A/B/C/D1-304[»]
2J5QX-ray2.15A/B/C/D1-304[»]
2J5RX-ray2.25A/B/C/D1-304[»]
2X0RX-ray2.92A/B1-304[»]
4JCOX-ray1.70A/B/C/D1-304[»]
ProteinModelPortalQ07841.
SMRQ07841. Positions 2-304.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC2706.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV47474; AAV47474; rrnAC2706.
GeneID3128541.
KEGGhma:rrnAC2706.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213793.
KOK00024.
OMACTADESK.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-2431-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.
ProtoNetSearch...

Other

EvolutionaryTraceQ07841.

Entry information

Entry nameMDH_HALMA
AccessionPrimary (citable) accession number: Q07841
Secondary accession number(s): Q5UZ29
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 14, 2014
This is version 120 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references