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Q60176 (MDH_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
EC=1.1.1.82
Gene names
Name:mdh
Synonyms:mdhB
Ordered Locus Names:MJ0490
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus ›

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate. Also catalyzes the reduction of sulfopyruvate, but not pyruvate, nor alpha-ketoglutarate. Higher selectivity for the coenzyme NADPH. Ref.2 Ref.3

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_00487

(S)-malate + NADP+ = oxaloacetate + NADPH. HAMAP-Rule MF_00487

Subunit structure

Homotetramer. Ref.4 Ref.5

Subcellular location

Cytoplasm HAMAP-Rule MF_00487.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113485

Regions

Nucleotide binding7 – 137NADP HAMAP-Rule MF_00487
Nucleotide binding34 – 374NADP HAMAP-Rule MF_00487
Nucleotide binding121 – 1233NADP HAMAP-Rule MF_00487

Sites

Active site1781Proton acceptor By similarity
Binding site861Substrate By similarity
Binding site921Substrate By similarity
Binding site991NADP
Binding site1231Substrate By similarity
Binding site1541Substrate By similarity

Secondary structure

1 ........................................................ 313
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60176 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: A7C0DB67C50151CC

FASTA31334,609
        10         20         30         40         50         60 
MKVTIIGASG RVGSATALLL AKEPFMKDLV LIGREHSINK LEGLREDIYD ALAGTRSDAN 

        70         80         90        100        110        120 
IYVESDENLR IIDESDVVII TSGVPRKEGM SRMDLAKTNA KIVGKYAKKI AEICDTKIFV 

       130        140        150        160        170        180 
ITNPVDVMTY KALVDSKFER NQVFGLGTHL DSLRFKVAIA KFFGVHIDEV RTRIIGEHGD 

       190        200        210        220        230        240 
SMVPLLSATS IGGIPIQKFE RFKELPIDEI IEDVKTKGEQ IIRLKGGSEF GPAAAILNVV 

       250        260        270        280        290        300 
RCIVNNEKRL LTLSAYVDGE FDGIRDVCIG VPVKIGRDGI EEVVSIELDK DEIIAFRKSA 

       310 
EIIKKYCEEV KNL

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii."
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. expand/collapse author list , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]"Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea."
Graupner M., Xu H., White R.H.
J. Bacteriol. 182:3688-3692(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[3]"The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase."
Madern D.
Mol. Microbiol. 37:1515-1520(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Differences in the oligomeric states of the LDH-like L-MalDH from the hyperthermophilic archaea Methanococcus jannaschii and Archaeoglobus fulgidus."
Madern D., Ebel C., Dale H.A., Lien T., Steen I.H., Birkeland N.-K., Zaccai G.
Biochemistry 40:10310-10316(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[5]"Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases."
Lee B.I., Chang C., Cho S.-J., Eom S.H., Kim K.K., Yu Y.G., Suh S.W.
J. Mol. Biol. 307:1351-1362(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L77117 Genomic DNA. Translation: AAB98481.1.
PIRB64361.
RefSeqNP_247466.1. NC_000909.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HYEX-ray1.90A1-313[»]
1HYGX-ray2.80A/B1-313[»]
ProteinModelPortalQ60176.
SMRQ60176. Positions 1-313.
ModBaseSearch...

Protein-protein interaction databases

STRING243232.MJ0490.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB98481; AAB98481; MJ_0490.
GeneID1451352.
KEGGmja:MJ_0490.

Phylogenomic databases

eggNOGCOG0039.
KOK00024.
OMADAMTYVM.
ProtClustDBPRK06223.

Enzyme and pathway databases

BRENDA1.1.1.272. 3263.
SABIO-RKQ60176.

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. Lactate_DH/Glyco_hydro_4_C. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ60176.

Entry information

Entry nameMDH_METJA
AccessionPrimary (citable) accession number: Q60176
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 29, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents