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

A1S3C4 (MDH_SHEAM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:Sama_0672
OrganismShewanella amazonensis (strain ATCC BAA-1098 / SB2B) [Complete proteome] [HAMAP]
Taxonomic identifier326297 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length311 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 – 311311Malate dehydrogenase HAMAP-Rule MF_01516
PRO_0000294300

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
A1S3C4 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 1FA1F95915B082C2

FASTA31132,021
        10         20         30         40         50         60 
MKVAVLGAAG GIGQALALLL KTQLPAGSKL SLYDIAPVTP GVAVDLSHIP TAVEVKGFCG 

        70         80         90        100        110        120 
EDPTPALEGA DVVLISAGVA RKPGMDRSDL FNINAGIVRN LIEKVAATCP KALVGIITNP 

       130        140        150        160        170        180 
VNTTVAIAAE VLKKAGVYDK NRLFGVTTLD VIRAETFVAE AKGVDVASVK VNVIGGHSGV 

       190        200        210        220        230        240 
TILPLLSQIE GVNFSDEEVA ALTKRIQNAG TEVVEAKAGG GSATLSMGQA AFRFGMSLIR 

       250        260        270        280        290        300 
GLQGEANVVE CAYVDGGSEH AVFFAQPVLL GKNGVEKVLP YGEVSAFEAN ARDAMLDTLK 

       310 
GDIQLGVDFV K 

« Hide

References

[1]"Complete sequence of Shewanella amazonensis SB2B."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1098 / SB2B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000507 Genomic DNA. Translation: ABL98880.1.
RefSeqYP_926550.1. NC_008700.1.

3D structure databases

ProteinModelPortalA1S3C4.
SMRA1S3C4. Positions 1-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326297.Sama_0672.

Proteomic databases

PRIDEA1S3C4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL98880; ABL98880; Sama_0672.
GeneID4602925.
KEGGsaz:Sama_0672.
PATRIC23449931. VBISheAma74963_0699.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213792.
KOK00024.
OMAVEVKGFA.
OrthoDBEOG6091FG.

Enzyme and pathway databases

BioCycSAMA326297:GH0T-702-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_SHEAM
AccessionPrimary (citable) accession number: A1S3C4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: February 6, 2007
Last modified: May 14, 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