[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-24. STRAIN=DSM 2088 / V24S; PubMed=2110059 [NCBI, ExPASy, EBI, Israel, Japan] Honka E., Fabry S., Niermann T., Palm P., Hensel R.; "Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus."; Eur. J. Biochem. 188:623-632(1990).
[2]	FUNCTION. DOI=10.1128/JB.182.13.3688-3692.2000; PubMed=10850983 [NCBI, ExPASy, EBI, Israel, Japan] Graupner M., Xu H., White R.H.; "Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea."; J. Bacteriol. 182:3688-3692(2000).

Comments

FUNCTION: Acts on oxaloacetate, sulfopyruvate but not on pyruvate. Has a higher selectivity for the coenzyme NADH than for NADPH.
CATALYTIC ACTIVITY: (S)-malate + NAD⁺ = oxaloacetate + NADH.
CATALYTIC ACTIVITY: (S)-malate + NADP⁺ = oxaloacetate + NADPH.
CATALYTIC ACTIVITY: (2R)-3-sulfolactate + NAD(P)⁺ = 3-sulfopyruvate + NAD(P)H.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X51714; CAA36010.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X51840; CAA36133.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S08981; S08981.

3D structure databases

ModBase

P16142.

Family and domain databases

InterPro

IPR003767; Malate/L-lactate_DHase.
Graphical view of domain structure.

PANTHER

PTHR11091; MDH_LDH; 1.

Pfam

PF02615; Ldh_2; 1.
Pfam graphical view of domain structure.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Direct protein sequencing; NAD; NADP; Oxidoreductase; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 339`	`339`		`Malate/L-sulfolactate dehydrogenase.`	`PRO_0000083827`

Sequence information

Length: 339 AA [This is the length of the unprocessed precursor]

Molecular weight: 36762 Da [This is the MW of the unprocessed precursor]

CRC64: 2319D822DB275835 [This is a checksum on the sequence]

        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

P16142 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools