Reviewed, UniProtKB/Swiss-Prot P80040 (MDH_CHLAA)

Names and origin

Protein names

Recommended name:
    Malate dehydrogenase
    EC=1.1.1.37

Gene names

Name:	mdh
Ordered Locus Names:	Caur_0900

Organism

Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl) [Complete proteome] [HAMAP]

Taxonomic identifier

324602 [NCBI]

Taxonomic lineage

Bacteria › Chloroflexi › Chloroflexales › Chloroflexaceae › Chloroflexus

Protein attributes

Sequence length	309 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. HAMAP MF_00487
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP MF_00487
Subunit structure	Homotetramer (active enzyme); homodimer and homotrimer at temperatures lower than 55 degrees Celsius (inactive forms). Ref.3 Ref.4 Ref.5
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 3 family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
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
Molecular function	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 – 309

309

Malate dehydrogenase HAMAP MF_00487

PRO_0000113447

Regions

Nucleotide binding

9 – 14

6

NAD HAMAP MF_00487

Nucleotide binding

118 – 120

3

NAD HAMAP MF_00487

Sites

Active site

175

1

Proton acceptor By similarity

Binding site

33

1

NAD HAMAP MF_00487

Binding site

82

1

Substrate HAMAP MF_00487

Binding site

88

1

Substrate HAMAP MF_00487

Binding site

95

1

NAD By similarity

Binding site

120

1

Substrate By similarity

Binding site

151

1

Substrate HAMAP MF_00487

Binding site

175

1

Substrate HAMAP MF_00487

Experimental info

Mutagenesis

187

1

T → C: Forms an intersubunit disulfide bridge, which makes the enzyme more resistant to thermal denaturation. The mutation does not alter the quaternary structure of the enzyme. HAMAP MF_00487

Sequence conflict

34

1

F → I in CAA61436. Ref.1

Sequence conflict

34

1

F → I Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

309

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Helix

12 – 23

12

Beta strand

27 – 32

6

Beta strand

34 – 37

4

Helix

38 – 47

10

Helix

50 – 53

4

Beta strand

59 – 63

5

Helix

65 – 68

4

Beta strand

72 – 76

5

Helix

92 – 106

15

Helix

107 – 109

3

Beta strand

114 – 117

4

Helix

122 – 133

12

Helix

137 – 139

3

Beta strand

140 – 142

3

Helix

145 – 160

16

Helix

164 – 166

3

Beta strand

167 – 169

3

Helix

176 – 178

3

Helix

183 – 185

3

Beta strand

186 – 188

3

Helix

193 – 195

3

Helix

199 – 210

12

Helix

212 – 220

9

Helix

227 – 241

15

Beta strand

246 – 256

11

Helix

257 – 259

3

Beta strand

261 – 272

12

Beta strand

275 – 279

5

Helix

286 – 305

20

Sequences

	Sequence		Length	Mass (Da)
	P80040-1 [UniParc]. Last modified March 18, 2008. Version 3. Checksum: AE1BACC5D5B36331	FASTA	309	32,751
	10 20 30 40 50 60 MRKKISIIGA GFVGSTTAHW LAAKELGDIV LLDFVEGVPQ GKALDLYEAS PIEGFDVRVT 70 80 90 100 110 120 GTNNYADTAN SDVIVVTSGA PRKPGMSRED LIKVNADITR ACISQAAPLS PNAVIIMVNN 130 140 150 160 170 180 PLDAMTYLAA EVSGFPKERV IGQAGVLDAA RYRTFIAMEA GVSVEDVQAM LMGGHGDEMV 190 200 210 220 230 240 PLPRFSTISG IPVSEFIAPD RLAQIVERTR KGGGEIVNLL KTGSAYYAPA AATAQMVEAV 250 260 270 280 290 300 LKDKKRVMPV AAYLTGQYGL NDIYFGVPVI LGAGGVEKIL ELPLNEEEMA LLNASAKAVR ATLDTLKSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Malate dehydrogenase from the green gliding bacterium Chloroflexus aurantiacus is phylogenetically related to lactic dehydrogenases." Synstad B., Emmerhoff O., Sirevag R. Arch. Microbiol. 165:346-353(1996) [PubMed: 8661927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of Chloroflexus aurantiacus J-10-fl." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Pierson B.K., Blankenship R.E., Richardson P. Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Malate dehydrogenase from the thermophilic green bacterium Chloroflexus aurantiacus: purification, molecular weight, amino acid composition, and partial amino acid sequence." Rolstad A.K., Howland E., Sirevag R. J. Bacteriol. 170:2947-2953(1988) [PubMed: 3133356] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-35, SUBUNIT.
[4]	"Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases." Dalhus B., Saarinen M., Sauer U.H., Eklund P., Johansson K., Karlsson A., Ramaswamy S., Bjoerk A., Synstad B., Naterstad K., Sirevaag R., Eklund H. J. Mol. Biol. 318:707-721(2002) [PubMed: 12054817] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 11-306 IN COMPLEX WITH NAD, SUBUNIT.
[5]	"Stabilization of a tetrameric malate dehydrogenase by introduction of a disulfide bridge at the dimer-dimer interface." Bjoerk A., Dalhus B., Mantzilas D., Eijsink V.G.H., Sirevaag R. J. Mol. Biol. 334:811-821(2003) [PubMed: 14636605] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANT CYS-187 IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X89038 Genomic DNA. Translation: CAA61436.1.
CP000909 Genomic DNA. Translation: ABY34133.1.

RefSeq

YP_001634522.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GUY	X-ray	2.20	A/C	1-309	[»]
1UR5	X-ray	1.75	A/C	1-309	[»]
1UXG	X-ray	1.90	A/B	1-309	[»]
1UXH	X-ray	2.10	A/B	1-309	[»]
1UXI	X-ray	2.10	A/B	1-309	[»]
1UXJ	X-ray	1.75	A/C	1-309	[»]
1UXK	X-ray	1.80	A/C	1-309	[»]

ModBase

Search...

Genome annotation databases

GeneID

5827960.

GenomeReviews

Gene locus Caur_0900 in contig CP000909_GR.

KEGG

cau:Caur_0900.

Organism-specific databases

CMR

Search...

Family and domain databases

HAMAP

MF_00487.
[Tree]

InterPro

IPR001557. L-lactate/malate_DH.
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.

TIGRFAMs

TIGR01763. MalateDH_bact. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MDH_CHLAA

Accession

Primary (citable) accession number: P80040
Secondary accession number(s): A9WH38

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	March 18, 2008
Last modified:	June 16, 2009
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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