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B0KMD1 (MDH_PSEPG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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:PputGB1_0697
OrganismPseudomonas putida (strain GB-1) [Complete proteome] [HAMAP]
Taxonomic identifier76869 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length309 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
   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 – 309309Malate dehydrogenase HAMAP-Rule MF_00487
PRO_1000191653

Regions

Nucleotide binding8 – 136NAD By similarity
Nucleotide binding118 – 1203NAD By similarity

Sites

Active site1751Proton acceptor By similarity
Binding site331NAD By similarity
Binding site821Substrate By similarity
Binding site881Substrate By similarity
Binding site951NAD By similarity
Binding site1201Substrate By similarity
Binding site1511Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B0KMD1 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: DB218AAD31586E46

FASTA30932,718
        10         20         30         40         50         60 
MNKLTIVGAG LVGEAAAQII ARDELCRELV LMDVQGELAQ GKALDVWQAA VESGSDTRVY 

        70         80         90        100        110        120 
GGAKAEMLDG SDLVVITAGV PRKPGQSRQD VLSINLPILD GIMTDIKHHA PAATVLVVSN 

       130        140        150        160        170        180 
PVDVLTYRAW SVSGLGRDKV FGQAGVLDTA RMKCFIAEQT GFSAKDITAL VLGGHGDSMV 

       190        200        210        220        230        240 
PLMRYCQIGS VPLSHFLSSE QIEQIVERTR KGGGEILGLK KMGSACDAPG VAIAQMVDAI 

       250        260        270        280        290        300 
ANGRNRILPA VAILQGEYGR KDIAMGVPCV LADEGLARVI ELPLDAQEQA MFDQSADQVA 


RDIDEMKAL 

« Hide

References

[1]"Complete sequence of Pseudomonas putida GB-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000926 Genomic DNA. Translation: ABY96607.1.
RefSeqYP_001666943.1. NC_010322.1.

3D structure databases

ProteinModelPortalB0KMD1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING76869.PputGB1_0697.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY96607; ABY96607; PputGB1_0697.
GeneID5868454.
KEGGppg:PputGB1_0697.
PATRIC19928351. VBIPsePut76638_0698.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAYAPSAFV.
OrthoDBEOG6091FG.

Enzyme and pathway databases

BioCycPPUT76869:GIXB-725-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.
ProtoNetSearch...

Entry information

Entry nameMDH_PSEPG
AccessionPrimary (citable) accession number: B0KMD1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 18, 2008
Last modified: May 14, 2014
This is version 43 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