Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P80040 (MDH_CHLAA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. 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:Caur_0900
OrganismChloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl) [Reference proteome] [HAMAP]
Taxonomic identifier324602 [NCBI]
Taxonomic lineageBacteriaChloroflexiChloroflexalesChloroflexaceaeChloroflexus

Protein attributes

Sequence length309 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 (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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113447

Regions

Nucleotide binding9 – 146NAD HAMAP-Rule MF_00487
Nucleotide binding118 – 1203NAD HAMAP-Rule MF_00487

Sites

Active site1751Proton acceptor By similarity
Binding site331NAD
Binding site821Substrate
Binding site881Substrate
Binding site951NAD By similarity
Binding site1201Substrate By similarity
Binding site1511Substrate
Binding site1751Substrate

Experimental info

Mutagenesis1871T → 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.
Sequence conflict341F → I in CAA61436. Ref.1
Sequence conflict341F → I Ref.3

Secondary structure

.......................................................... 309
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80040 [UniParc].

Last modified March 18, 2008. Version 3.
Checksum: AE1BACC5D5B36331

FASTA30932,751
        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 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of the filamentous anoxygenic phototrophic bacterium Chloroflexus aurantiacus."
Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J., Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W., Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.
BMC Genomics 12:334-334(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29366 / DSM 635 / J-10-fl.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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

EMBL
GenBank
DDBJ
X89038 Genomic DNA. Translation: CAA61436.1.
CP000909 Genomic DNA. Translation: ABY34133.1.
RefSeqYP_001634522.1. NC_010175.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GUYX-ray2.20A/C1-309[»]
1UR5X-ray1.75A/C1-309[»]
1UXGX-ray1.90A/B1-309[»]
1UXHX-ray2.10A/B1-309[»]
1UXIX-ray2.10A/B1-309[»]
1UXJX-ray1.75A/C1-309[»]
1UXKX-ray1.80A/C1-309[»]
4CL3X-ray1.70A/D1-309[»]
ProteinModelPortalP80040.
SMRP80040. Positions 2-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING324602.Caur_0900.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY34133; ABY34133; Caur_0900.
GeneID5827960.
KEGGcau:Caur_0900.
PATRIC21412507. VBIChlAur28763_1031.

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OrthoDBEOG6091FG.
ProtClustDBPRK06223.

Enzyme and pathway databases

BioCycCAUR324602:GIXU-910-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

EvolutionaryTraceP80040.

Entry information

Entry nameMDH_CHLAA
AccessionPrimary (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: April 16, 2014
This is version 113 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