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Q822E9 (MDH_CHLCV) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:CCA_00734
OrganismChlamydophila caviae (strain GPIC) [Complete proteome] [HAMAP]
Taxonomic identifier227941 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_01517

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_01517

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01517

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 2 family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcellular 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-HAMAP

   Molecular_functionL-malate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000113356

Regions

Nucleotide binding15 – 217NAD By similarity
Nucleotide binding133 – 1353NAD By similarity

Sites

Active site1911Proton acceptor By similarity
Binding site961Substrate By similarity
Binding site1021Substrate By similarity
Binding site1091NAD By similarity
Binding site1161NAD By similarity
Binding site1351Substrate By similarity
Binding site1661Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q822E9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D3E0544E1146AD5C

FASTA33036,083
        10         20         30         40         50         60 
MIMKLMRTVS VAVTGGTGQI AYSFLFALAH GDVFGSDCSI DLRVYDLPGL ERALSGVRME 

        70         80         90        100        110        120 
LDDCAYPLLQ SLRVTTSLED ACDGIDAAFL IGAAPRGPGM ERSDLLKRNG EIFSLQGSVL 

       130        140        150        160        170        180 
NVCAKRDAKI FVVGNPVNTN CWIAMNKAPK LNRRNFHSML RLDQNRMHTM LAHRAEVPLD 

       190        200        210        220        230        240 
EVTNVVVWGN HSAKQVPDFT QALISGKPAV EVISDRDWLE NIMFPSIQNR GSAVIEARGK 

       250        260        270        280        290        300 
SSAGSAARAL AEAARSIFLP KDGEWFSSGV CSDYNPYGIP DDLIFGFPCR MLPSGDYEIV 

       310        320        330 
PGLPWDAFIK NKIQISLDEI SQEKASVSLL 

« Hide

References

[1]"Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G. expand/collapse author list , Rank R.G., Bavoil P.M., Fraser C.M.
Nucleic Acids Res. 31:2134-2147(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GPIC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015925 Genomic DNA. Translation: AAP05475.1.
RefSeqNP_829597.1. NC_003361.3.

3D structure databases

ProteinModelPortalQ822E9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227941.CCA00734.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP05475; AAP05475; CCA_00734.
GeneID1218419.
KEGGcca:CCA00734.
PATRIC20270593. VBIChlCav107360_0780.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
KOK00024.
OMACRMLPSG.
OrthoDBEOG6PP9Q2.
ProtClustDBPRK05442.

Enzyme and pathway databases

BioCycCCAV227941:GH8L-763-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_01517. Malate_dehydrog_2.
InterProIPR001557. 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]
PANTHERPTHR23382. PTHR23382. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01759. MalateDH-SF1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMDH_CHLCV
AccessionPrimary (citable) accession number: Q822E9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 81 of the entry and version 1 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