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P16142 (MDH_METFV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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/(S)-sulfolactate dehydrogenase

EC=1.1.1.310
EC=1.1.1.37
EC=1.1.1.82
Gene names
Name:mdh
Ordered Locus Names:Mfer_0389
OrganismMethanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S) [Complete proteome] [HAMAP]
Taxonomic identifier523846 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanothermaceaeMethanothermus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts on oxaloacetate, sulfopyruvate but not on pyruvate. Has a higher selectivity for the coenzyme NADH than for NADPH. Ref.3

Catalytic activity

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

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

(2S)-3-sulfolactate + NAD+ = 3-sulfopyruvate + NADH.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the LDH2/MDH2 oxidoreductase family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processtricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-malate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

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 – 339339Malate/(S)-sulfolactate dehydrogenase
PRO_0000083827

Sequences

Sequence LengthMass (Da)Tools
P16142 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: 2319D822DB275835

FASTA33936,762
        10         20         30         40         50         60 
MIISPEEERS LIIKILNALG VSEEHAKITA DVIVDADLKG FTSHGIGRFP QYVEGIKLGT 

        70         80         90        100        110        120 
IKTSGNIEIE KETDSVALIN GNHLLGQVVA YKGMKLAIEK AKNTGVGIVG IHDSNHFGIA 

       130        140        150        160        170        180 
GYYSDMAMKN DMIGITMTNT EPAVAPLGGK IPVLGTNPIA ISIPSNEYYV AVDMSTAAVA 

       190        200        210        220        230        240 
RGKLLEAARK NEKIPEGIAV DKNGNPTTDP NEALNGSILP FGGHKGYALC FMIEILAGPL 

       250        260        270        280        290        300 
VKAEFGSKVK GTVDPSQMCT KGDLLIAIDP SKFYDIEEFK RNVDEFVKEI KSTGKDVLIP 

       310        320        330 
GDRERMNIKK REKEGIELDK KLVEKLKEIA DELNIELTW 

« Hide

References

« Hide 'large scale' references
[1]"Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus."
Honka E., Fabry S., Niermann T., Palm P., Hensel R.
Eur. J. Biochem. 188:623-632(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-24.
Strain: ATCC 43054 / DSM 2088 / JCM 10308 / V24 S.
[2]"Complete genome sequence of Methanothermus fervidus type strain (V24S)."
Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S., Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N. expand/collapse author list , Pati A., Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M., Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.
Stand. Genomic Sci. 3:315-324(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43054 / DSM 2088 / JCM 10308 / V24 S.
[3]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51714 Genomic DNA. Translation: CAA36010.1.
X51840 Genomic DNA. Translation: CAA36133.1.
CP002278 Genomic DNA. Translation: ADP77191.1.
PIRS08981.
RefSeqYP_004003953.1. NC_014658.1.

3D structure databases

ProteinModelPortalP16142.
SMRP16142. Positions 1-338.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADP77191; ADP77191; Mfer_0389.
GeneID9962106.
KEGGmfv:Mfer_0389.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000173270.
KOK05884.
OMAENGNINP.

Enzyme and pathway databases

BioCycMFER523846:GC24-404-MONOMER.
SABIO-RKP16142.

Family and domain databases

InterProIPR003767. Malate/L-lactate_DH.
[Graphical view]
PANTHERPTHR11091. PTHR11091. 1 hit.
PfamPF02615. Ldh_2. 1 hit.
[Graphical view]
SUPFAMSSF89733. SSF89733. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMDH_METFV
AccessionPrimary (citable) accession number: P16142
Secondary accession number(s): E3GY09
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: August 1, 1990
Last modified: May 14, 2014
This is version 73 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