Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9YEA1 (MDH_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 97. 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
EC=1.1.1.82
Gene names
Name:mdh
Ordered Locus Names:APE_0672.1
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length308 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate. Can also oxidize tartrate. Can utilize both NAD and NADP. Has a preference for NADP. Ref.2

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. Ref.2

(S)-malate + NADP+ = oxaloacetate + NADPH. Ref.2

Subunit structure

Homotetramer. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00487.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=0.019 mM for S-malate (in the presence of NADP) Ref.2

KM=0.12 mM for S-malate (in the presence of NAD)

KM=1.2 mM for (2S,3S)-tartrate (in the presence of NAD)

KM=23 mM for (2S,3S)-tartrate (in the presence of NADP)

KM=5.8 mM for (2S,3R)-tartrate (in the presence of NADP)

KM=0.2 mM for (2S,3R)-tartrate (in the presence of NAD)

KM=0.87 mM for NAD (in the presence of malate)

KM=0.0076 mM for NAD (in the presence of malate)

pH dependence:

Optimum pH is 11 for malate oxidation.

Temperature dependence:

Optimum temperature is 95 degrees Celsius.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete 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-malate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

malate dehydrogenase (NADP+) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 308308Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113479

Regions

Nucleotide binding6 – 116NAD By similarity
Nucleotide binding115 – 1173NAD By similarity

Sites

Active site1721Proton acceptor By similarity
Binding site791Substrate By similarity
Binding site851Substrate By similarity
Binding site921NAD By similarity
Binding site1171Substrate By similarity
Binding site1481Substrate By similarity

Secondary structure

.................................................... 308
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9YEA1 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: C2A14F224650B8CE

FASTA30833,490
        10         20         30         40         50         60 
MITILGAGKV GMATAVMLMM RGYDDLLLIA RTPGKPQGEA LDLAHAAAEL GVDIRISGSN 

        70         80         90        100        110        120 
SYEDMRGSDI VLVTAGIGRK PGMTREQLLE ANANTMADLA EKIKAYAKDA IVVITTNPVD 

       130        140        150        160        170        180 
AMTYVMYKKT GFPRERVIGF SGILDSARMA YYISQKLGVS FKSVNAIVLG MHGQKMFPVP 

       190        200        210        220        230        240 
RLSSVGGVPL EHLMSKEEIE EVVSETVNAG AKITELRGYS SNYGPAAGLV LTVEAIKRDS 

       250        260        270        280        290        300 
KRIYPYSLYL QGEYGYNDIV AEVPAVIGKS GIERIIELPL TEDEKRKFDE AVQAVKKLVE 


TLPPQLRE 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1."
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. expand/collapse author list , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.
DNA Res. 6:83-101(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.
[2]"Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix."
Kawakami R., Sakuraba H., Goda S., Tsuge H., Ohshima T.
Biochim. Biophys. Acta 1794:1496-1504(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS), SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000002 Genomic DNA. Translation: BAA79645.2.
PIRE72655.
RefSeqNP_147405.2. NC_000854.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D4AX-ray2.87A/B/C/D1-308[»]
ProteinModelPortalQ9YEA1.
SMRQ9YEA1. Positions 1-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272557.APE_0672.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA79645; BAA79645; APE_0672.1.
GeneID1444806.
KEGGape:APE_0672.1.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
ProtClustDBPRK06223.

Enzyme and pathway databases

BioCycAPER272557:GJD6-489-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...

Other

EvolutionaryTraceQ9YEA1.

Entry information

Entry nameMDH_AERPE
AccessionPrimary (citable) accession number: Q9YEA1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 26, 2007
Last modified: February 19, 2014
This is version 97 of the entry and version 2 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