Reviewed, UniProtKB/Swiss-Prot P16142 (MDH_METFE)

Names and origin

Protein names

Recommended name:
    Malate/L-sulfolactate dehydrogenase
    EC=1.1.1.37
    EC=1.1.1.82
    EC=1.1.1.272
Alternative name(s):
    (R)-2-hydroxyacid dehydrogenase

Gene names

Name:

mdh

Organism

Methanothermus fervidus

Taxonomic identifier

2180 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanothermaceae › Methanothermus

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.2
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. (S)-malate + NADP+ = oxaloacetate + NADPH. (2R)-3-sulfolactate + NAD(P)+ = 3-sulfopyruvate + NAD(P)H.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the LDH2/MDH2 oxidoreductase family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	(R)-2-hydroxyacid dehydrogenase activity Inferred from electronic annotation. Source: EC L-malate dehydrogenase activity Inferred from electronic annotation. Source: EC malate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 339	339	Malate/L-sulfolactate dehydrogenase		PRO_0000083827

Sequences

	Sequence		Length	Mass (Da)
	P16142-1 [UniParc]. Last modified August 1, 1990. Version 2. Checksum: 2319D822DB275835	FASTA	339	36,762
	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

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: 2110059] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-24. Strain: DSM 2088 / V24S.
[2]	"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: 10850983] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X51714 Genomic DNA. Translation: CAA36010.1. X51840 Genomic DNA. Translation: CAA36133.1.
PIR	S08981.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.272. 7358. 1.1.1.37. 7358. 1.1.1.82. 7358.
Family and domain databases
InterPro	IPR003767. Malate/L-lactate_DH. [Graphical view]
PANTHER	PTHR11091. MDH_LDH. 1 hit.
Pfam	PF02615. Ldh_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDH_METFE

Accession

Primary (citable) accession number: P16142

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	August 1, 1990
Last modified:	June 16, 2009
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)