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P61976 (MDH_MYCPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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:MAP_2541c
OrganismMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) [Complete proteome] [HAMAP]
Taxonomic identifier262316 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length329 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 – 329329Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000113379

Regions

Nucleotide binding12 – 187NAD By similarity
Nucleotide binding130 – 1323NAD By similarity

Sites

Active site1881Proton acceptor By similarity
Binding site931Substrate By similarity
Binding site991Substrate By similarity
Binding site1061NAD By similarity
Binding site1131NAD By similarity
Binding site1321Substrate By similarity
Binding site1631Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P61976 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: F640765FD4A7DD84

FASTA32934,631
        10         20         30         40         50         60 
MSASPLKVAV TGAAGQIGYS LLFRLASGSL LGPDRPIELR LLEIEPALKA LEGVVMELDD 

        70         80         90        100        110        120 
CAFPLLSGVE IGADPNKIFD GANLALLVGA RPRGPGMERS DLLEANGAIF TAQGKALNEV 

       130        140        150        160        170        180 
AADDIRVGVT GNPANTNALI AMSNAPDIPR ERFSALTRLD HNRAISQLAK KTGAKVTDIK 

       190        200        210        220        230        240 
KMTIWGNHSA TQYPDIFHAE VKGKNAAEVV GDQNWIENDF IPTVAKRGAA IIDARGASSA 

       250        260        270        280        290        300 
ASAASATTDA ARDWLLGTPA GDWVSMAVIS DGSYGVPEGL ISSFPVTTKD GDWTIVQGLE 

       310        320 
IDEFSRSRID KTTAELADER NAVTQLGLI 

« Hide

References

[1]"The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-968 / K-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016958 Genomic DNA. Translation: AAS04858.1.
RefSeqNP_961475.1. NC_002944.2.

3D structure databases

ProteinModelPortalP61976.
SMRP61976. Positions 4-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262316.MAP2541c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS04858; AAS04858; MAP_2541c.
GeneID2719157.
KEGGmpa:MAP2541c.
PATRIC17997766. VBIMycAvi108102_2697.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
KOK00024.
OMACRMLPSG.
OrthoDBEOG6PP9Q2.
ProtClustDBPRK05442.

Enzyme and pathway databases

BioCycMAVI262316:GCQR-2577-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.
IPR001252. Malate_DH_AS.
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.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_MYCPA
AccessionPrimary (citable) accession number: P61976
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: February 19, 2014
This is version 75 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