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A1T9L9 (MDH_MYCVP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:Mvan_3067
OrganismMycobacterium vanbaalenii (strain DSM 7251 / PYR-1) [Complete proteome] [HAMAP]
Taxonomic identifier350058 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length332 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 – 332332Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000292373

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 site1351Substrate By similarity
Binding site1661Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1T9L9 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 318F708372599FB7

FASTA33234,506
        10         20         30         40         50         60 
MSSTTASPVT VAVTGAAGHI GYAALFRIAA GAMLGHTTPV TLRLLELPDA VRAAEGVVME 

        70         80         90        100        110        120 
LEDGAFPLLA GTEIYDDPTR AFDGVDVALL IGARPRTKGM ERADLLGANA EIFATSGKAL 

       130        140        150        160        170        180 
NAGASPDVRV LVVGNPANTN ALVASAHAPD IPADRFTALT RLDHNRAVAA TARHSGVPVT 

       190        200        210        220        230        240 
EISRMTIWGN HSPTQYPDIF HAVVGGRSGA DYAADTRWLT DDFIPTVARR GTAIIEARGA 

       250        260        270        280        290        300 
SSAASAANGA IDHIDDWVHG TPDGDWTSVA LPSPGAYGVD EGLVCSFPCR SVGGRWEIVE 

       310        320        330 
GLDINPFSRA RIDASVAELR TERDAVAALG LL 

« Hide

References

[1]"Complete sequence of Mycobacterium vanbaalenii PYR-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.J., Miller C., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 7251 / PYR-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000511 Genomic DNA. Translation: ABM13869.1.
RefSeqYP_953875.1. NC_008726.1.

3D structure databases

ProteinModelPortalA1T9L9.
SMRA1T9L9. Positions 6-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING350058.Mvan_3067.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM13869; ABM13869; Mvan_3067.
GeneID4646973.
KEGGmva:Mvan_3067.
PATRIC18184407. VBIMycVan31953_3125.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMAFPDYRHA.
OrthoDBEOG6PP9Q2.

Enzyme and pathway databases

BioCycMVAN350058:GIWR-3086-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_MYCVP
AccessionPrimary (citable) accession number: A1T9L9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 51 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