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P80039 (MDH_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Malate dehydrogenase

EC=1.1.1.37
Gene names
Name:mdh
Ordered Locus Names:CT1507
OrganismChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS) [Reference proteome] [HAMAP]
Taxonomic identifier194439 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate. HAMAP-Rule MF_00487

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 310310Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113448

Regions

Nucleotide binding7 – 126NAD HAMAP-Rule MF_00487
Nucleotide binding117 – 1193NAD HAMAP-Rule MF_00487

Sites

Active site1741Proton acceptor By similarity
Binding site321NAD
Binding site811Substrate By similarity
Binding site871Substrate By similarity
Binding site941NAD
Binding site1191Substrate By similarity
Binding site1501Substrate By similarity

Experimental info

Sequence conflict2271A → S in CAA56810. Ref.1

Secondary structure

....................................................... 310
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80039 [UniParc].

Last modified August 30, 2002. Version 3.
Checksum: 30A92ACFE9442A93

FASTA31033,092
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80838 Genomic DNA. Translation: CAA56810.1.
AE006470 Genomic DNA. Translation: AAM72734.1.
RefSeqNP_662392.1. NC_002932.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GUZX-ray2.00A/B/C/D1-71[»]
1GV0X-ray2.50A/B1-310[»]
ProteinModelPortalP80039.
SMRP80039. Positions 1-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING194439.CT1507.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM72734; AAM72734; CT1507.
GeneID1007223.
KEGGcte:CT1507.
PATRIC21400925. VBIChlTep116050_1367.

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAYGQNDIC.
OrthoDBEOG6091FG.

Enzyme and pathway databases

BioCycCTEP194439:GHN0-1546-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_00487. Malate_dehydrog_3.
InterProIPR001557. 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]
PANTHERPTHR11540. PTHR11540. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSPR00086. LLDHDRGNASE.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01763. MalateDH_bact. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP80039.

Entry information

Entry nameMDH_CHLTE
AccessionPrimary (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: July 9, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references