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A3MWU9 (MDH_PYRCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:Pcal_1699
OrganismPyrobaculum calidifontis (strain JCM 11548 / VA1) [Complete proteome] [HAMAP]
Taxonomic identifier410359 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length309 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 – 309309Malate dehydrogenase HAMAP-Rule MF_00487
PRO_1000026483

Regions

Nucleotide binding6 – 116NAD By similarity
Nucleotide binding116 – 1183NAD By similarity

Sites

Active site1731Proton acceptor By similarity
Binding site311NAD By similarity
Binding site801Substrate By similarity
Binding site861Substrate By similarity
Binding site931NAD By similarity
Binding site1181Substrate By similarity
Binding site1491Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A3MWU9 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 04CB46D8FD7EEBCB

FASTA30933,293
        10         20         30         40         50         60 
MITIVGSGRV GTAAAAIMGI MRIDKKILLI DIVKGLPQGE ALDLNHMSAI LGLDVEYEGS 

        70         80         90        100        110        120 
NDYKDMAGSD LVIVTAGFPR KPGMTREQLV ETNAKIVSDI GKEIKKYAPD SVVILTTNPL 

       130        140        150        160        170        180 
DAMTYVMWKS TGFPRERVIG FSGVLDAGRL AYYAAKKLGI SPASILPIVL GQHGESMFPV 

       190        200        210        220        230        240 
PSKSFVHGVP LSKLLSEDQL REVVEETVKA GAKITELRGF SSNWGPGAGL AIMADSVKRD 

       250        260        270        280        290        300 
ARRSLIASVV LKGEYGVFDL PVEVPIVLGK TGVVKVLEIE LTPEEKEKFN QSVEAIRKLV 


GTIPQSYLQ 

« Hide

References

[1]"Complete sequence of Pyrobaculum calidifontis JCM 11548."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 11548 / VA1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000561 Genomic DNA. Translation: ABO09116.1.
RefSeqYP_001056582.1. NC_009073.1.

3D structure databases

ProteinModelPortalA3MWU9.
SMRA3MWU9. Positions 1-307.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING410359.Pcal_1699.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO09116; ABO09116; Pcal_1699.
GeneID4909393.
KEGGpcl:Pcal_1699.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAYGQNDIC.

Enzyme and pathway databases

BioCycPCAL410359:GIX2-1735-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...

Entry information

Entry nameMDH_PYRCJ
AccessionPrimary (citable) accession number: A3MWU9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: May 14, 2014
This is version 49 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