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

A7GTN7 (MDH_BACCN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:Bcer98_3276
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_00487

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 3 family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandNAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   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 – 312312Malate dehydrogenase HAMAP-Rule MF_00487
PRO_1000081352

Regions

Nucleotide binding12 – 176NAD By similarity
Nucleotide binding123 – 1253NAD By similarity

Sites

Active site1801Proton acceptor By similarity
Binding site361NAD By similarity
Binding site871Substrate By similarity
Binding site931Substrate By similarity
Binding site1001NAD By similarity
Binding site1251Substrate By similarity
Binding site1561Substrate By similarity

Amino acid modifications

Modified residue1491Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7GTN7 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 01CAD84DDCDEADBE

FASTA31233,737
        10         20         30         40         50         60 
MTIKRKKVSV IGAGFTGATT AFLLAQKELA DVVLVDIPQL ENPTKGKALD MLEASPVQGF 

        70         80         90        100        110        120 
DANIIGTSDY ADTADSDVVI ITAGIARKPG MSRDDLVATN SKIMKSVTKE IAKHSPDTII 

       130        140        150        160        170        180 
IVLTNPVDAM TYSVFKEAGF PKERVIGQSG VLDTARFRTF IAQELNLSVK DITGFVLGGH 

       190        200        210        220        230        240 
GDDMVPLVRY SYAGGIPLET LISKERLDAI VERTRKGGGE IVNLLGNGSA YYAPAASLVE 

       250        260        270        280        290        300 
MTEAILKDQR RVLPAIAYLE GEYGYRDLYL GVPVILGGNG IEKVIELELR EEEKMALDRS 

       310 
VESVRNVMEI LS 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NVH 391-98.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000764 Genomic DNA. Translation: ABS23495.1.
RefSeqYP_001376490.1. NC_009674.1.

3D structure databases

ProteinModelPortalA7GTN7.
SMRA7GTN7. Positions 5-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315749.Bcer98_3276.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS23495; ABS23495; Bcer98_3276.
GeneID5345777.
KEGGbcy:Bcer98_3276.
PATRIC18935196. VBIBacCyt128034_3439.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAGANSYEA.
OrthoDBEOG6091FG.
ProtClustDBPRK06223.

Enzyme and pathway databases

BioCycBCYT315749:GH2A-3386-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...

Entry information

Entry nameMDH_BACCN
AccessionPrimary (citable) accession number: A7GTN7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 11, 2007
Last modified: February 19, 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