Reviewed, UniProtKB/Swiss-Prot P19446 (MDHG_CITLA)

Names and origin

Protein names	Recommended name:     Malate dehydrogenase, glyoxysomal     EC=1.1.1.37
Organism	Citrullus lanatus (Watermelon) (Citrullus vulgaris)
Taxonomic identifier	3654 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Cucurbitales › Cucurbitaceae › Citrullus

Protein attributes

Sequence length	356 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)

Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH.
Subunit structure	Homodimer. Ref.3
Subcellular location	Glyoxysome.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 1 family.
Biophysicochemical properties	Kinetic parameters: KM=146 µM for NADH KM=76 mM for oxaloacetate

Ontologies

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Cellular component	Glyoxysome
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: InterPro glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW 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: UniProtKB-KW
Cellular component	glyoxysome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: EC 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

Transit peptide

1 – 36

36

Glyoxysome Ref.2

Chain

37 – 356

320

Malate dehydrogenase, glyoxysomal

PRO_0000018638

Regions

Nucleotide binding

51 – 57

7

NAD By similarity

Nucleotide binding

160 – 162

3

NAD By similarity

Sites

Active site

220

1

Proton acceptor

Binding site

77

1

NAD By similarity

Binding site

124

1

Substrate

Binding site

130

1

Substrate

Binding site

137

1

NAD By similarity

Binding site

162

1

Substrate

Binding site

196

1

Substrate

Binding site

271

1

NAD By similarity

Secondary structure

1

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356

Helix Strand Turn

Details...

Beta strand

45 – 51

7

Helix

57 – 65

9

Beta strand

70 – 80

11

Helix

81 – 89

9

Beta strand

96 – 102

7

Helix

103 – 110

8

Beta strand

114 – 118

5

Beta strand

130 – 132

3

Helix

133 – 151

19

Beta strand

155 – 159

5

Helix

164 – 176

13

Turn

177 – 179

3

Beta strand

185 – 188

4

Helix

191 – 204

14

Helix

209 – 211

3

Beta strand

216 – 218

3

Helix

222 – 224

3

Beta strand

225 – 227

3

Helix

229 – 231

3

Helix

240 – 251

12

Helix

253 – 260

8

Turn

261 – 263

3

Helix

269 – 287

19

Beta strand

292 – 299

8

Beta strand

301 – 315

15

Beta strand

318 – 322

5

Helix

330 – 354

25

Sequences

	Sequence		Length	Mass (Da)
	P19446-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 4B0C8101DC11FC7F	FASTA	356	37,637
	10 20 30 40 50 60 MQPIPDVNQR IARISAHLHP PKSQMEESSA LRRANCRAKG GAPGFKVAIL GAAGGIGQPL 70 80 90 100 110 120 AMLMKMNPLV SVLHLYDVVN APGVTADISH MDTGAVVRGF LGQQQLEAAL TGMDLIIVPA 130 140 150 160 170 180 GVPRKPGMTR DDLFKINAGI VKTLCEGIAK CCPRAIVNLI SNPVNSTVPI AAEVFKKAGT 190 200 210 220 230 240 YDPKRLLGVT MLDVVRANTF VAEVLGLDPR DVDVPVVGGH AGVTILPLLS QVKPPSSFTQ 250 260 270 280 290 300 EEISYLTDRI QNGGTEVVEA KAGAGSATLS MAYAAVKFAD ACLRGLRGDA GVIECAFVSS 310 320 330 340 350 QVTELPFFAS KVRLGRNGIE EVYSLGPLNE YERIGLEKAK KELAGSIEKG VSFIRS

References

[1]	"Glyoxysomal malate dehydrogenase from watermelon is synthesized with an amino-terminal transit peptide." Gietl C. Proc. Natl. Acad. Sci. U.S.A. 87:5773-5777(1990) [PubMed: 2377615] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: cv. Sugar Baby.
[2]	"Sequence homologies between glyoxysomal and mitochondrial malate dehydrogenase." Gietl C., Lottspeich F., Hock B. Planta 169:555-558(1986) Cited for: PROTEIN SEQUENCE OF 37-65.
[3]	"Organelle and translocatable forms of glyoxysomal malate dehydrogenase. The effect of the N-terminal presequence." Cox B., Chit M.M., Weaver T., Gietl C., Bailey J., Bell E., Banaszak L. FEBS J. 272:643-654(2005) [PubMed: 15670147] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS, X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, PHYSICOCHEMICAL PROPERTIES, SUBUNIT, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M33148 mRNA. Translation: AAA33041.1.

PIR

DEPUGW. A35957.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SEV	X-ray	2.55	A/B	1-356	[»]
1SMK	X-ray	2.50	A/B/C/D/E/F/G/H	37-356	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.1.1.37. 81664.

Family and domain databases

InterPro

IPR001557. L-lactate/malate_DH.
IPR001236. Lactate/malate_DH.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR010097. Malate_DH_NAD-dep_euk_g_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.

PANTHER

PTHR11540:SF1. MDH_euk_g_bac. 1 hit.

Pfam

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

PIRSF

PIRSF000102. Lac_mal_DH. 1 hit.

TIGRFAMs

TIGR01772. MDH_euk_gproteo. 1 hit.

PROSITE

PS00068. MDH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MDHG_CITLA

Accession

Primary (citable) accession number: P19446

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)