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

Q3IFH4 (MDH_PSEHT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:PSHAa2658
OrganismPseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]
Taxonomic identifier326442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_01516

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_01516

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01516

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 1 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 – 310310Malate dehydrogenase HAMAP-Rule MF_01516
PRO_0000294298

Regions

Nucleotide binding7 – 137NAD By similarity
Nucleotide binding117 – 1193NAD By similarity

Sites

Active site1771Proton acceptor By similarity
Binding site341NAD By similarity
Binding site811Substrate By similarity
Binding site871Substrate By similarity
Binding site941NAD By similarity
Binding site1191Substrate By similarity
Binding site1531Substrate By similarity
Binding site2271NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3IFH4 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 73CFE950275B0A13

FASTA31031,920
        10         20         30         40         50         60 
MKVAVLGAAG GIGQALSLLL KTGLPAGSEL SLYDVAPVVP GVAVDLSHIP TAVKVAGFGA 

        70         80         90        100        110        120 
DALNEALKDA DIVLIPAGMP RKPGMDRADL FNVNAGIIKT LAEGIVASCP KALVGIITNP 

       130        140        150        160        170        180 
VNGTVPIVAE VFKKAGTYDA KRVFGITTLD VIRSEAFVAE LKGVDVATVK VPVIGGHSGT 

       190        200        210        220        230        240 
TILPLLSQVE GVSFTDEEVA ALTPRIQNAG TEVVNAKAGG GSATLSMGAA AARFCMSLVK 

       250        260        270        280        290        300 
GLQGEDVVDY AYVAVENGDA EYFAHPVRLG KNGVEEILSY GELSAFETKA KNDMLETLKK 

       310 
DIKEGVDFMA 

« Hide

References

[1]"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125."
Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. expand/collapse author list , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.
Genome Res. 15:1325-1335(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TAC 125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR954246 Genomic DNA. Translation: CAI87706.1.
RefSeqYP_341148.1. NC_007481.1.

3D structure databases

ProteinModelPortalQ3IFH4.
SMRQ3IFH4. Positions 1-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326442.PSHAa2658.

Proteomic databases

PRIDEQ3IFH4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI87706; CAI87706; PSHAa2658.
GeneID3710235.
KEGGpha:PSHAa2658.
PATRIC32298901. VBIPseHal105694_2568.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213792.
KOK00024.
OMAVEVKGFA.
OrthoDBEOG6091FG.
ProtClustDBPRK05086.

Enzyme and pathway databases

BioCycPHAL326442:GJIU-2713-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_01516. Malate_dehydrog_1.
InterProIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR010097. Malate_DH_type1.
IPR023958. Malate_DH_type1_bac.
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.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_PSEHT
AccessionPrimary (citable) accession number: Q3IFH4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: November 8, 2005
Last modified: February 19, 2014
This is version 63 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