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Q817F9 (MDH_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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:BC_4592
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP]
Taxonomic identifier226900 [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
Reference 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_0000113426

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
Q817F9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 73CA61C603BD17E2

FASTA31233,512
        10         20         30         40         50         60 
MTIKRKKVSV IGAGFTGATT AFLLAQKELA DVVLVDIPQL ENPTKGKALD MLEASPVQGF 

        70         80         90        100        110        120 
DANIIGTSDY ADTADSDVVV ITAGIARKPG MSRDDLVATN SKIMKSITRD IAKHSPNAII 

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

       190        200        210        220        230        240 
GDDMVPLVRY SYAGGIPLET LIPKERLEAI VERTRKGGGE IVGLLGNGSA YYAPAASLVE 

       250        260        270        280        290        300 
MTEAILKDQR RILPAIAYLE GEYGYSDLYL GVPVILGGNG IEKIIELELL ADEKEALDRS 

       310 
VESVRNVMKV LV 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP11499.1.
RefSeqNP_834298.1. NC_004722.1.

3D structure databases

ProteinModelPortalQ817F9.
SMRQ817F9. Positions 5-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226900.BC4592.

Proteomic databases

PRIDEQ817F9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP11499; AAP11499; BC_4592.
GeneID1206937.
KEGGbce:BC4592.
PATRIC32605311. VBIBacCer54481_4754.

Phylogenomic databases

eggNOGCOG0039.
KOK00024.
OMAGANSYEA.
OrthoDBEOG6091FG.
ProtClustDBPRK06223.

Enzyme and pathway databases

BioCycBCER226900:GJEU-4588-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_BACCR
AccessionPrimary (citable) accession number: Q817F9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 83 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