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Q0K8F5 (MDH_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:H16_A2634
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_01517

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_01517

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01517

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 2 family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete 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

   Molecular_functionL-malate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 327326Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000294401

Regions

Nucleotide binding12 – 187NAD By similarity
Nucleotide binding130 – 1323NAD By similarity

Sites

Active site1881Proton acceptor By similarity
Binding site931Substrate By similarity
Binding site991Substrate By similarity
Binding site1061NAD By similarity
Binding site1131NAD By similarity
Binding site1321Substrate By similarity
Binding site1631Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0K8F5 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 24B1BF5CAD4A3190

FASTA32735,102
        10         20         30         40         50         60 
MAKAPMRVAV TGAAGQIGYS LLFRIANGDM LGKDQPVILQ LLDLPQAQQA VKGVVMELED 

        70         80         90        100        110        120 
CAFPLLAGVV ITDDPKVAFK DADVALLVGA RPRSKGMERK DLLEANAQIF TVQGKALDEV 

       130        140        150        160        170        180 
ASRNVKVLVV GNPANTNAYI AMKSAPNLPR ENFTAMLRLD HNRALSQIAA KTGKPVSSIE 

       190        200        210        220        230        240 
KLFVWGNHSP TMYADYRYAT VDGKSVKDLI NDPVWNNDVF LPTVGKRGAA IIEARGLSSA 

       250        260        270        280        290        300 
ASAANAAIDH VRDWVLGTNG KVVTMGIPSN GEYGIPADTM FGYPVTTANG KYEIVKGLEI 

       310        320 
DAYSQEKINI TLNELEEEKA GVQHLLG 

« Hide

References

[1]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260479 Genomic DNA. Translation: CAJ93716.1.
RefSeqYP_727084.1. NC_008313.1.

3D structure databases

ProteinModelPortalQ0K8F5.
SMRQ0K8F5. Positions 3-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.H16_A2634.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ93716; CAJ93716; H16_A2634.
GeneID4250055.
KEGGreh:H16_A2634.
PATRIC35234777. VBIRalEut6770_3022.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMANCLIASK.
OrthoDBEOG6PP9Q2.
ProtClustDBPRK05442.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-2601-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_01517. Malate_dehydrog_2.
InterProIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR23382. PTHR23382. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01759. MalateDH-SF1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMDH_CUPNH
AccessionPrimary (citable) accession number: Q0K8F5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: October 3, 2006
Last modified: February 19, 2014
This is version 54 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