Reviewed, UniProtKB/Swiss-Prot Q60176 (MDH_METJA)

Names and origin

Protein names

Recommended name:
    Malate dehydrogenase
    EC=1.1.1.37
    EC=1.1.1.82

Gene names

Name:	mdh
Synonyms:	mdhB
Ordered Locus Names:	MJ0490

Organism

Methanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP]

Taxonomic identifier

2190 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the reversible oxidation of malate to oxaloacetate. Also catalyzes the reduction of sulfopyruvate, but not pyruvate, nor alpha-ketoglutarate. Higher selectivity for the coenzyme NADPH.
Catalytic activity	(S)-malate + NAD(+) = oxaloacetate + NADH. (S)-malate + NADP(+) = oxaloacetate + NADPH.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 3 family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP binding Inferred from electronic annotation. Source: InterPro 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 – 313

313

Malate dehydrogenase

PRO_0000113485

Regions

Nucleotide binding

7 – 13

7

NADP

Nucleotide binding

34 – 37

4

NADP

Nucleotide binding

121 – 123

3

NADP

Sites

Active site

178

1

Proton acceptor By similarity

Binding site

86

1

Substrate By similarity

Binding site

92

1

Substrate By similarity

Binding site

99

1

NADP

Binding site

123

1

Substrate By similarity

Binding site

154

1

Substrate By similarity

Secondary structure

1

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313

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Turn

7 – 9

3

Helix

11 – 21

11

Beta strand

28 – 33

6

Helix

35 – 37

3

Helix

38 – 52

15

Beta strand

60 – 65

6

Helix

69 – 72

4

Beta strand

76 – 80

5

Helix

92 – 113

22

Beta strand

117 – 120

4

Beta strand

122 – 124

3

Helix

125 – 136

12

Beta strand

142 – 145

4

Helix

149 – 163

15

Helix

167 – 169

3

Beta strand

174 – 176

3

Beta strand

182 – 184

3

Helix

186 – 188

3

Helix

196 – 198

3

Helix

200 – 204

5

Helix

207 – 217

11

Helix

232 – 244

13

Beta strand

249 – 263

15

Beta strand

265 – 276

12

Beta strand

279 – 283

5

Helix

290 – 310

21

Sequences

	Sequence		Length	Mass (Da)
	Q60176-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: A7C0DB67C50151CC	FASTA	313	34,609
	10 20 30 40 50 60 MKVTIIGASG RVGSATALLL AKEPFMKDLV LIGREHSINK LEGLREDIYD ALAGTRSDAN 70 80 90 100 110 120 IYVESDENLR IIDESDVVII TSGVPRKEGM SRMDLAKTNA KIVGKYAKKI AEICDTKIFV 130 140 150 160 170 180 ITNPVDVMTY KALVDSKFER NQVFGLGTHL DSLRFKVAIA KFFGVHIDEV RTRIIGEHGD 190 200 210 220 230 240 SMVPLLSATS IGGIPIQKFE RFKELPIDEI IEDVKTKGEQ IIRLKGGSEF GPAAAILNVV 250 260 270 280 290 300 RCIVNNEKRL LTLSAYVDGE FDGIRDVCIG VPVKIGRDGI EEVVSIELDK DEIIAFRKSA 310 EIIKKYCEEV KNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[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.
[3]	"The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase." Madern D. Mol. Microbiol. 37:1515-1520(2000) [PubMed: 10998181] [Abstract] Cited for: FUNCTION.
[4]	"Differences in the oligomeric states of the LDH-like L-MalDH from the hyperthermophilic archaea Methanococcus jannaschii and Archaeoglobus fulgidus." Madern D., Ebel C., Dale H.A., Lien T., Steen I.H., Birkeland N.-K., Zaccai G. Biochemistry 40:10310-10316(2001) [PubMed: 11513609] [Abstract] Cited for: SUBUNIT.
[5]	"Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases." Lee B.I., Chang C., Cho S.-J., Eom S.H., Kim K.K., Yu Y.G., Suh S.W. J. Mol. Biol. 307:1351-1362(2001) [PubMed: 11292347] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L77117 Genomic DNA. Translation: AAB98481.1.

PIR

B64361.

RefSeq

NP_247466.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HYE	X-ray	1.90	A	1-313	[»]
1HYG	X-ray	2.80	A/B	1-313	[»]

ModBase

Search...

Genome annotation databases

GeneID

1451352.

GenomeReviews

Gene locus MJ0490 in contig L77117_GR.

KEGG

mja:MJ0490.

NMPDR

fig|243232.1.peg.503.

TIGR

MJ0490.

Phylogenomic databases

HOGENOM

Q60176.

Enzyme and pathway databases

BioCyc

MJAN243232:MJ_0490-MON.

Family and domain databases

HAMAP

MF_00487.
[Tree]

InterPro

IPR001557. L-lactate/malate_DHase.
IPR001236. Lactate/malate_DHase.
IPR015955. Lactate_DHase/Glyco_Ohase_4_C.
IPR016040. NAD(P)-bd.
[Graphical view]

Gene3D

G3DSA:3.90.110.10. lact_mal_DH. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000102. Lac_mal_DH. 1 hit.

PRINTS

PR00086. LLDHDRGNASE.

ProtoNet

Search...

Entry information

Entry name

MDH_METJA

Accession

Primary (citable) accession number: Q60176

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	November 25, 2008
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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