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O08349 (MDH_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 118. 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:AF_0855
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length294 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

Homodimer. Ref.3

Subcellular location

Cytoplasm HAMAP-Rule MF_00487.

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
Reference 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

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-lactate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

L-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 – 294294Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113480

Regions

Nucleotide binding7 – 126NAD HAMAP-Rule MF_00487
Nucleotide binding117 – 1193NAD HAMAP-Rule MF_00487

Sites

Active site1721Proton acceptor
Binding site321NAD
Binding site811Substrate By similarity
Binding site871Substrate By similarity
Binding site941NAD
Binding site1191Substrate By similarity
Binding site1501Substrate By similarity

Secondary structure

..................................................... 294
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O08349 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 90389DBC189B944F

FASTA29431,874
        10         20         30         40         50         60 
MKLGFVGAGR VGSTSAFTCL LNLDVDEIAL VDIAEDLAVG EAMDLAHAAA GIDKYPKIVG 

        70         80         90        100        110        120 
GADYSLLKGS EIIVVTAGLA RKPGMTRLDL AHKNAGIIKD IAKKIVENAP ESKILVVTNP 

       130        140        150        160        170        180 
MDVMTYIMWK ESGKPRNEVF GMGNQLDSQR LKERLYNAGA RNIRRAWIIG EHGDSMFVAK 

       190        200        210        220        230        240 
SLADFDGEVD WEAVENDVRF VAAEVIKRKG ATIFGPAVAI YRMVKAVVED TGEIIPTSMI 

       250        260        270        280        290 
LQGEYGIENV AVGVPAKLGK NGAEVADIKL SDEEIEKLRN SAKILRERLE ELGY 

« Hide

References

« Hide 'large scale' references
[1]"Properties and primary structure of a thermostable L-malate dehydrogenase from Archaeoglobus fulgidus."
Langelandsvik A.S., Steen I.H., Birkeland N.K., Lien T.
Arch. Microbiol. 168:59-67(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. expand/collapse author list , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[3]"The 2.9A resolution crystal structure of malate dehydrogenase from Archaeoglobus fulgidus: mechanisms of oligomerisation and thermal stabilisation."
Irimia A., Vellieux F.M.D., Madern D., Zaccai G., Karshikoff A., Tibbelin G., Ladenstein R., Lien T., Birkeland N.-K.
J. Mol. Biol. 335:343-356(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z85985 Genomic DNA. Translation: CAB06654.1.
AE000782 Genomic DNA. Translation: AAB90384.1.
PIRG69356.
RefSeqNP_069689.1. NC_000917.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2X0IX-ray2.90A1-294[»]
2X0JX-ray2.79A1-294[»]
ProteinModelPortalO08349.
SMRO08349. Positions 1-294.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224325.AF0855.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB90384; AAB90384; AF_0855.
GeneID1484074.
KEGGafu:AF0855.

Phylogenomic databases

eggNOGCOG0039.
KOK00024.
OMAYAPSAFV.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-873-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.
IPR018177. L-lactate_DH_AS.
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

EvolutionaryTraceO08349.

Entry information

Entry nameMDH_ARCFU
AccessionPrimary (citable) accession number: O08349
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: May 14, 2014
This is version 118 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