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Q6L0C3 (MDH_PICTO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. 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:PTO0994
OrganismPicrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828) [Complete proteome] [HAMAP]
Taxonomic identifier263820 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesPicrophilaceaePicrophilus

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete 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 – 324324Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113490

Regions

Nucleotide binding10 – 156NAD By similarity
Nucleotide binding124 – 1263NAD By similarity

Sites

Active site1811Proton acceptor By similarity
Binding site341NAD By similarity
Binding site881Substrate By similarity
Binding site941Substrate By similarity
Binding site1011NAD By similarity
Binding site1261Substrate By similarity
Binding site1571Substrate By similarity

Secondary structure

...................................................... 324
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6L0C3 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 86937A7F6AC89D4C

FASTA32435,215
        10         20         30         40         50         60 
MARSKISVIG AGAVGATVAQ TLAIRQTGDI YIFDIVDGLA EGKALDILEG APHWGYDLDI 

        70         80         90        100        110        120 
KGFCTADESK YAEMKGSDVI VVTAGLARKP GMSRDDLLLK NIGIMKSVGE AIKKYSPESK 

       130        140        150        160        170        180 
IVVVTNPADI MAYAIYKASG ISPERIIGLG GSLDSTRFRT FLAQELNVSF EDVNAFVIGG 

       190        200        210        220        230        240 
HGDDMVPFIR YSNVSGIPIE DLLPREKIDE IVKRTRFGGG EIVNLYKTGS AFYAPGISIA 

       250        260        270        280        290        300 
VMVESIVNDR KRVIPCAAYI TGEHSKTYLV NNLFIGVPIK IGKNGVEKIY DLKFNEDELE 

       310        320 
AWKKSVESVK KNSAIADDYF AKNQ 

« Hide

References

[1]"Genome sequence of Picrophilus torridus and its implications for life around pH 0."
Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C., Schepers B., Dock C., Antranikian G., Liebl W.
Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017261 Genomic DNA. Translation: AAT43579.1.
RefSeqYP_023772.1. NC_005877.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BGVX-ray1.81A/B/C/D2-324[»]
ProteinModelPortalQ6L0C3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING263820.PTO0994.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT43579; AAT43579; PTO0994.
GeneID2844444.
KEGGpto:PTO0994.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMACTADESK.

Enzyme and pathway databases

BioCycPTOR263820:GHA3-1036-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_PICTO
AccessionPrimary (citable) accession number: Q6L0C3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 76 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