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Q9K849 (MDH_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 100. 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
Synonyms:citH
Ordered Locus Names:BH3158
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length314 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 – 314314Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113429

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
Q9K849 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 02D132F11E3B8E34

FASTA31433,681
        10         20         30         40         50         60 
MAIKRRKVSV IGAGFTGATT ALMVAQKELG DVVLVDIPQM EGPTKGKALD MLESTPVQGV 

        70         80         90        100        110        120 
DVNITGTSSY EYTKDSDVVV ITAGIARKPG MSRDDLVSTN AGIMKAVTKE VVKHSPNAYI 

       130        140        150        160        170        180 
IVLTNPADAM TYTVYKESGF PKNRVIGQSG VLDTARFRTF VAQELNLSVE DITGFVLGGH 

       190        200        210        220        230        240 
GDDMVPLIRY SYAGGIPLEK LLPQERIDAI VERTRKGGGE IVGLLGNGSA YYAPAASLAE 

       250        260        270        280        290        300 
MVEAILKDKK RVLPTIAYLE GEYGYEDIYV GVPTILGGDG IEKVIELDLT DEEKATFAKS 

       310 
IESVRNVMSA LPKE 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB06877.1.
PIRF84044.
RefSeqNP_244024.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9K849.
SMRQ9K849. Positions 5-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH3158.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB06877; BAB06877; BAB06877.
GeneID890638.
KEGGbha:BH3158.
PATRIC18943572. VBIBacHal18977_3285.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMASANEHEK.
OrthoDBEOG6091FG.
ProtClustDBPRK06223.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-3257-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_BACHD
AccessionPrimary (citable) accession number: Q9K849
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 100 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