Reviewed, UniProtKB/Swiss-Prot O08349 (MDH_ARCFU)

Names and origin

Protein names

Recommended name:
    Malate dehydrogenase
    EC=1.1.1.37

Gene names

Name:	mdh
Ordered Locus Names:	AF_0855

Organism

Archaeoglobus fulgidus [Complete proteome] [HAMAP]

Taxonomic identifier

2234 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

Protein attributes

Sequence length	294 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the reversible oxidation of malate to oxaloacetate. HAMAP MF_00487
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP MF_00487
Subunit structure	Homodimer. Ref.3
Subcellular location	Cytoplasm HAMAP MF_00487.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 3 family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: InterPro malate metabolic process 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-SubCell
Molecular function	L-lactate dehydrogenase activity Inferred from electronic annotation. Source: InterPro L-malate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 294

294

Malate dehydrogenase HAMAP MF_00487

PRO_0000113480

Regions

Nucleotide binding

7 – 12

6

NAD HAMAP MF_00487

Nucleotide binding

117 – 119

3

NAD HAMAP MF_00487

Sites

Active site

172

1

Proton acceptor HAMAP MF_00487

Binding site

32

1

NAD HAMAP MF_00487

Binding site

81

1

Substrate By similarity

Binding site

87

1

Substrate By similarity

Binding site

94

1

NAD HAMAP MF_00487

Binding site

119

1

Substrate By similarity

Binding site

150

1

Substrate By similarity

Secondary structure

1

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294

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

10 – 22

13

Beta strand

26 – 31

6

Helix

35 – 50

16

Turn

51 – 53

3

Beta strand

57 – 62

6

Helix

64 – 67

4

Beta strand

71 – 75

5

Helix

87 – 106

20

Beta strand

113 – 116

4

Beta strand

118 – 120

3

Helix

121 – 131

11

Beta strand

138 – 141

4

Helix

144 – 157

14

Beta strand

168 – 173

6

Helix

180 – 182

3

Helix

191 – 209

19

Helix

214 – 228

15

Beta strand

234 – 243

10

Helix

244 – 246

3

Beta strand

248 – 259

12

Beta strand

262 – 265

4

Helix

272 – 290

19

Turn

291 – 293

3

Sequences

	Sequence		Length	Mass (Da)
	O08349-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 90389DBC189B944F	FASTA	294	31,874
	10 20 30 40 50 60 MKLGFVGAGR VGSTSAFTCL LNLDVDEIAL VDIAEDLAVG EAMDLAHAAA GIDKYPKIVG 70 80 90 100 110 120 GADYSLLKGS EIIVVTAGLA RKPGMTRLDL AHKNAGIIKD IAKKIVENAP ESKILVVTNP 130 140 150 160 170 180 MDVMTYIMWK ESGKPRNEVF GMGNQLDSQR LKERLYNAGA RNIRRAWIIG EHGDSMFVAK 190 200 210 220 230 240 SLADFDGEVD WEAVENDVRF VAAEVIKRKG ATIFGPAVAI YRMVKAVVED TGEIIPTSMI 250 260 270 280 290 LQGEYGIENV AVGVPAKLGK NGAEVADIKL SDEEIEKLRN SAKILRERLE ELGY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Properties and primary structure of a thermostable L-malate dehydrogenase from Archaeoglobus fulgidus." Langelandsvik A.S., Steen I.H., Birkeland N.K., Lien T. Arch. Microbiol. 168:59-67(1997) [PubMed: 9211715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]	"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Nature 390:364-370(1997) [PubMed: 9389475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[3]	"The 2.9A resolution crystal structure of malate dehydrogenase from Archaeoglobus fulgidus: mechanisms of oligomerisation and thermal stabilisation." Irimia A., Vellieux F.M.D., Madern D., Zaccai G., Karshikoff A., Tibbelin G., Ladenstein R., Lien T., Birkeland N.-K. J. Mol. Biol. 335:343-356(2004) [PubMed: 14659762] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z85985 Genomic DNA. Translation: CAB06654.1.
AE000782 Genomic DNA. Translation: AAB90384.1.

PIR

G69356.

RefSeq

NP_069689.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2X0I	X-ray	2.90	A	1-294	[»]
2X0J	X-ray	2.79	A	1-294	[»]

ModBase

Search...

Genome annotation databases

GeneID

1484074.

GenomeReviews

Gene locus AF_0855 in contig AE000782_GR.

KEGG

afu:AF0855.

NMPDR

fig|224325.1.peg.848.

TIGR

AF_0855.

Phylogenomic databases

HOGENOM

HBG566126.

OMA

DAMTYVM.

Enzyme and pathway databases

BioCyc

AFUL224325:AF_0855-MONOMER.

BRENDA

1.1.1.37. 7576.

Family and domain databases

HAMAP

MF_00487. Malate_dehydrog_3.
[Tree]

InterPro

IPR001557. L-lactate/malate_DH.
IPR018177. L-lactate_DH_AS.
IPR001236. Lactate/malate_DH.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR011275. Malate_DH_NAD-dep_bac.
IPR016040. NAD(P)-bd_dom.
[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_ARCFU

Accession

Primary (citable) accession number: O08349

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	July 1, 1997
Last modified:	February 9, 2010
This is version 91 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)