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

Q8TWG5 (MDH_METKA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. 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:MK1069
OrganismMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) [Reference proteome] [HAMAP]
Taxonomic identifier190192 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_00487

Catalytic activity

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

Subcellular location

Cytoplasm By similarity 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 termComplete 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 – 317317Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113486

Regions

Nucleotide binding8 – 147NAD By similarity
Nucleotide binding121 – 1233NAD By similarity

Sites

Active site1781Proton acceptor By similarity
Binding site851Substrate By similarity
Binding site911Substrate By similarity
Binding site981NAD By similarity
Binding site1231Substrate By similarity
Binding site1541Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8TWG5 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: D2AC04B7C0B6C26E

FASTA31734,609
        10         20         30         40         50         60 
MSKVAVIGAT GRVGSTAAAR LALLDCVNEV TLIARPKSVD KLRGLRRDIL DSLAAAQKDA 

        70         80         90        100        110        120 
EITIGCERDD YVDADVIVMT AGIPRKPGQT RLDLTKDNAA IIKKYLEGVA EENPEAIVLV 

       130        140        150        160        170        180 
VTNPVDVLTY VALKVSGLPK NRVIGLGTHL DSMRFKVLIA KHFNVHMSEV HTRIIGEHGD 

       190        200        210        220        230        240 
TMVPVISSTS VGGIPVTRMP GWEDFDVEEA VREVKEAGQR IIETWGGSQF GPAQAITNLV 

       250        260        270        280        290        300 
RTILQDERRV LTVSAYLDGE IDGIRDVCIG VPARLGREGV LEIVPIELEE DEMRAFRRSV 

       310 
KVVKEATREA MEAISER 

« Hide

References

[1]"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009439 Genomic DNA. Translation: AAM02282.1.
RefSeqNP_614352.1. NC_003551.1.

3D structure databases

ProteinModelPortalQ8TWG5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190192.MK1069.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM02282; AAM02282; MK1069.
GeneID1477170.
KEGGmka:MK1069.

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213793.
KOK00024.
OMAITIGCER.

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...

Entry information

Entry nameMDH_METKA
AccessionPrimary (citable) accession number: Q8TWG5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: June 1, 2002
Last modified: May 14, 2014
This is version 82 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