Q9ZF99 (MDH_AQUAR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Malate dehydrogenase
EC=1.1.1.37

Gene names

Name:

mdh

Organism

Aquaspirillum arcticum

Taxonomic identifier

87645 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Oxalobacteraceae

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP MF_01517
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP MF_01517
Subunit structure	Homodimer. Ref.1
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 2 family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro malate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide 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

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 329

328

Malate dehydrogenase HAMAP MF_01517

PRO_0000113346

Regions

Nucleotide binding

12 – 18

7

NAD HAMAP MF_01517

Nucleotide binding

132 – 134

3

NAD HAMAP MF_01517

Sites

Active site

190

1

Proton acceptor

Binding site

95

1

Substrate By similarity

Binding site

101

1

Substrate By similarity

Binding site

108

1

NAD By similarity

Binding site

115

1

NAD

Binding site

134

1

Substrate By similarity

Binding site

165

1

Substrate

Secondary structure

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329

Helix Strand Turn

Details...

Beta strand

6 – 12

7

Helix

16 – 26

11

Turn

27 – 31

5

Beta strand

37 – 42

6

Helix

47 – 61

15

Turn

62 – 64

3

Beta strand

68 – 76

9

Helix

77 – 80

4

Turn

81 – 83

3

Beta strand

85 – 89

5

Helix

101 – 122

22

Beta strand

128 – 131

4

Beta strand

133 – 135

3

Helix

136 – 145

10

Helix

152 – 154

3

Beta strand

155 – 157

3

Helix

160 – 174

15

Helix

178 – 180

3

Beta strand

181 – 183

3

Beta strand

185 – 188

4

Beta strand

195 – 197

3

Helix

208 – 212

5

Helix

215 – 220

6

Helix

222 – 227

6

Helix

229 – 237

9

Helix

242 – 258

17

Beta strand

265 – 270

6

Helix

274 – 276

3

Beta strand

282 – 290

9

Beta strand

293 – 296

4

Helix

304 – 324

21

Helix

325 – 328

4

Sequences

	Sequence		Length	Mass (Da)
	Q9ZF99 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F02E2826E5028F27	FASTA	329	35,251
	10 20 30 40 50 60 MAKTPMRVAV TGAAGQICYS LLFRIANGDM LGKDQPVILQ LLEIPNEKAQ KALQGVMMEI 70 80 90 100 110 120 DDCAFPLLAG MTAHADPMTA FKDADVALLV GARPRGPGME RKDLLEANAQ IFTVQGKAID 130 140 150 160 170 180 AVASRNIKVL VVGNPANTNA YIAMKSAPSL PAKNFTAMLR LDHNRALSQI AAKTGKPVSS 190 200 210 220 230 240 IEKLFVWGNH SPTMYADYRY AQIDGASVKD MINDDAWNRD TFLPTVGKRG AAIIDARGVS 250 260 270 280 290 300 SAASAANAAI DHIHDWVLGT AGKWTTMGIP SDGSYGIPEG VIFGFPVTTE NGEYKIVQGL 310 320 SIDAFSQERI NVTLNELLEE QNGVQHLLG

References

[1]

"Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum." Kim S.-Y., Hwang K.Y., Kim S.-H., Sung H.-C., Han Y.S., Cho Y. J. Biol. Chem. 274:11761-11767(1999) [PubMed: 10206992] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22 AND 103-123, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF109682 Genomic DNA. Translation: AAD13225.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B8P	X-ray	1.90	A	1-329	[»]
1B8U	X-ray	2.50	A	1-329	[»]
1B8V	X-ray	2.10	A	1-329	[»]

ProteinModelPortal

Q9ZF99.

SMR

Q9ZF99. Positions 3-329.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

HAMAP

MF_01517. Malate_dehydrog_2.
[Tree]

InterPro

IPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR010945. Malate_DH_type2.
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.

PANTHER

PTHR23382. MDH_SF1. 1 hit.

Pfam

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

PIRSF

PIRSF000102. Lac_mal_DH. 1 hit.

SUPFAM

SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.

TIGRFAMs

TIGR01759. MalateDH-SF1. 1 hit.

PROSITE

PS00068. MDH. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MDH_AQUAR

Accession

Primary (citable) accession number: Q9ZF99

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program