P80039 (MDH_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Malate dehydrogenase
EC=1.1.1.37

Gene names

Name:	mdh
Ordered Locus Names:	CT1507

Organism

Chlorobium tepidum

Taxonomic identifier

1097 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum

Protein attributes

Sequence length	310 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	Homotetramer; arranged as a dimer of dimers. Ref.4
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 Reference proteome
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

Chain

1 – 310

310

Malate dehydrogenase HAMAP MF_00487

PRO_0000113448

Regions

Nucleotide binding

7 – 12

6

NAD HAMAP MF_00487

Nucleotide binding

117 – 119

3

NAD HAMAP MF_00487

Sites

Active site

174

1

Proton acceptor By similarity

Binding site

32

1

NAD

Binding site

81

1

Substrate By similarity

Binding site

87

1

Substrate By similarity

Binding site

94

1

NAD

Binding site

119

1

Substrate By similarity

Binding site

150

1

Substrate By similarity

Experimental info

Sequence conflict

227

1

A → S in CAA56810. Ref.1

Secondary structure

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310

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

10 – 22

13

Beta strand

26 – 31

6

Beta strand

33 – 36

4

Helix

37 – 46

10

Helix

49 – 52

4

Beta strand

57 – 62

6

Helix

64 – 67

4

Beta strand

71 – 75

5

Helix

92 – 105

14

Turn

106 – 108

3

Beta strand

113 – 116

4

Beta strand

118 – 120

3

Helix

121 – 132

12

Helix

136 – 138

3

Beta strand

139 – 142

4

Helix

144 – 159

16

Helix

163 – 165

3

Beta strand

166 – 172

7

Helix

175 – 177

3

Beta strand

178 – 187

10

Helix

192 – 194

3

Helix

198 – 209

12

Helix

211 – 219

9

Beta strand

220 – 222

3

Helix

226 – 240

15

Beta strand

245 – 255

11

Helix

256 – 258

3

Beta strand

260 – 271

12

Beta strand

274 – 278

5

Helix

285 – 304

20

Sequences

	Sequence		Length	Mass (Da)
	P80039 [UniParc]. Last modified August 30, 2002. Version 3. Checksum: 30A92ACFE9442A93	FASTA	310	33,092
	10 20 30 40 50 60 MKITVIGAGN VGATTAFRLA EKQLARELVL LDVVEGIPQG KALDMYESGP VGLFDTKVTG 70 80 90 100 110 120 SNDYADTANS DIVVITAGLP RKPGMTREDL LSMNAGIVRE VTGRIMEHSK NPIIVVVSNP 130 140 150 160 170 180 LDIMTHVAWQ KSGLPKERVI GMAGVLDSAR FRSFIAMELG VSMQDVTACV LGGHGDAMVP 190 200 210 220 230 240 VVKYTTVAGI PVADLISAER IAELVERTRT GGAEIVNHLK QGSAFYAPAT SVVEMVESIV 250 260 270 280 290 300 LDRKRVLTCA VSLDGQYGID GTFVGVPVKL GKNGVEHIYE IKLDQSDLDL LQKSAKIVDE 310 NCKMLDASQG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Malate dehydrogenase from the mesophile Chlorobium vibrioforme and from the mild thermophile Chlorobium tepidum: molecular cloning, construction of a hybrid, and expression in Escherichia coli." Naterstad K., Lauvrak V., Sirevag R. J. Bacteriol. 178:7047-7052(1996) [PubMed: 8955383] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium." Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. , Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed: 12093901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49652 / DSM 12025 / TLS.
[3]	"Malate dehydrogenase from Chlorobium vibrioforme, Chlorobium tepidum, and Heliobacterium gestii: purification, characterization, and investigation of dinucleotide binding by dehydrogenases by use of empirical methods of protein sequence analysis." Charnock C.B., Refseth U.H., Strevaag R. J. Bacteriol. 174:1307-1313(1992) [PubMed: 1735722] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-34.
[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 (2.5 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X80838 Genomic DNA. Translation: CAA56810.1.
AE006470 Genomic DNA. Translation: AAM72734.1.

RefSeq

NP_662392.1. NC_002932.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GUZ	X-ray	2.00	A/B/C/D	1-305	[»]
1GV0	X-ray	2.50	A/B	1-310	[»]

ProteinModelPortal

P80039.

SMR

P80039. Positions 1-305.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1007223.

GenomeReviews

Gene locus CT1507 in contig AE006470_GR.

KEGG

cte:CT1507.

NMPDR

fig|194439.1.peg.1486.

PATRIC

21400925. VBIChlTep116050_1367.

TIGR

CT1507.

Phylogenomic databases

HOGENOM

HBG566126.

OMA

ANSYEAI.

ProtClustDB

PRK06223.

Enzyme and pathway databases

BioCyc

CTEP194439:CT_1507-MONOMER.

Family and domain databases

HAMAP

MF_00487. Malate_dehydrog_3.
[Tree]

InterPro

IPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR011275. Malate_DH_type3.
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.

KO

K00024.

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.

SUPFAM

SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.

TIGRFAMs

TIGR01763. MalateDH_bact. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MDH_CHLTE

Accession

Primary (citable) accession number: P80039
Secondary accession number(s): P94677

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	August 30, 2002
Last modified:	January 25, 2012
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program