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Reviewed, UniProtKB/Swiss-Prot O08349 (MDH_ARCFU)

Last modified November 25, 2008. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Malate dehydrogenase
    EC=1.1.1.37
Gene names
Name: mdh
Ordered Locus Names: AF_0855
OrganismArchaeoglobus fulgidus [Complete proteome] [HAMAP]
Taxonomic identifier2234 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate.

Catalytic activity

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

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

Gene Ontology (GO)

   Biological processglycolysis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

tricarboxylic acid cycle

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionL-malate dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Malate dehydrogenase
PRO_0000113480

Regions

Nucleotide binding7 – 126NAD
Nucleotide binding117 – 1193NAD

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
O08349-1 [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: 9211715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[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: 9389475] [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: 14659762] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.

Cross-references

Sequence databases

Z85985 Genomic DNA. Translation: CAB06654.1.
AE000782 Genomic DNA. Translation: AAB90384.1.
PIRG69356.
RefSeqNP_069689.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1OJSX-ray2.91A1-294[»]
1OJUX-ray2.79A1-294[»]
ModBaseSearch...

Genome annotation databases

GeneID1484074.
GenomeReviewsGene locus AF_0855 in contig AE000782_GR.
KEGGafu:AF0855.
NMPDRfig|224325.1.peg.848.
TIGRAF_0855.

Phylogenomic databases

HOGENOMO08349.

Enzyme and pathway databases

BioCycAFUL224325:AF_0855-MON.

Family and domain databases

HAMAPMF_00487.
[Tree]
InterProIPR001557. L-lactate/malate_DHase.
IPR001236. Lactate/malate_DHase.
IPR015955. Lactate_DHase/Glyco_Ohase_4_C.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.90.110.10. lact_mal_DH. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSPR00086. LLDHDRGNASE.
ProtoNetSearch...

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: November 25, 2008
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents