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P11386 (MDH_SULAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 98. 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:Saci_0246
OrganismSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) [Complete proteome] [HAMAP]
Taxonomic identifier330779 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity.

Catalytic activity

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

Sequence similarities

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

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcellular carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionL-malate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 306305Malate dehydrogenase
PRO_0000113492

Regions

Nucleotide binding8 – 136NAD By similarity
Nucleotide binding118 – 1203NAD By similarity

Sites

Active site1721Proton acceptor By similarity
Binding site331NAD By similarity
Binding site821Substrate By similarity
Binding site881Substrate By similarity
Binding site951NAD By similarity
Binding site1201Substrate By similarity
Binding site1481Substrate By similarity

Experimental info

Sequence conflict111R → RG AA sequence Ref.2
Sequence conflict40 – 423EKF → TKK AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P11386 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E74C0CB278B3BA89

FASTA30633,563
        10         20         30         40         50         60 
MVKVAFIGVG RVGQTIAYNT IVNGYADEVM LYDVVPELPE KFEHEIRHAL AALRVKTELL 

        70         80         90        100        110        120 
STNNIDDISG ADIVVITAGK PRKPGMSRRD LFIDNAKIMI DLAKKLPKKN KGAMYIMVAN 

       130        140        150        160        170        180 
PVDMMASVFM KYSGENTIST GNQVETMRMR SYIAKKLNIP AYEVGGYVGG EHGEAAMVLW 

       190        200        210        220        230        240 
STVTVKGKPF SESLGVNKAE VEDYVKKIAA EIIRVLGGTT WGPGADIEEV IRSVALNEGK 

       250        260        270        280        290        300 
VMSVAFPHKY EDEIIHISEP VVVGRTVGPA LTSALDENDK ARLSQAIKEV YNVYKSNLKE 


LEQVIS 

« Hide

References

« Hide 'large scale' references
[1]"The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota."
Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.
J. Bacteriol. 187:4992-4999(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.
[2]"Archaebacterial malate dehydrogenase: the amino-terminal sequence of the enzyme from Sulfolobus acidocaldarius is homologous to the eubacterial and eukaryotic malate dehydrogenases."
Gorisch H., Jany K.-D.
FEBS Lett. 247:259-262(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-42.
Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000077 Genomic DNA. Translation: AAY79663.1.
PIRS03958.
RefSeqYP_254956.1. NC_007181.1.

3D structure databases

ProteinModelPortalP11386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING330779.Saci_0246.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY79663; AAY79663; Saci_0246.
GeneID3474728.
KEGGsai:Saci_0246.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213793.
KOK00024.
OMADITPFMG.
ProtClustDBCLSK883804.

Enzyme and pathway databases

BioCycSACI330779:GH9J-244-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
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_SULAC
AccessionPrimary (citable) accession number: P11386
Secondary accession number(s): Q4JC16
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 98 of the entry and version 3 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