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Q0I491 (MDH_HISS1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:HS_1055
OrganismHistophilus somni (strain 129Pt) (Haemophilus somnus) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

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_0000294296

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
Q0I491 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: A415E60EB754527D

FASTA31132,543
        10         20         30         40         50         60 
MKIAVLGAAG GIGQALALLL KLQLPAGSEL SLYDIAPVTP GVAADVSHIP TAVKIQGFAG 

        70         80         90        100        110        120 
EDPTPALENA DVVLISAGVA RKPGMDRSDL FNINAGIVKN LIEKVAKTCP KACVGIITNP 

       130        140        150        160        170        180 
VNTTVAIAAE VLKKAGVYDK RKLFGVTTLD VLRSETFVAE LKGLNVSRIA VPVIGGHSGV 

       190        200        210        220        230        240 
TILPLLSQVQ YAEWEEDEIA PLTKRIQNAG TEVVEAKAGG GSATLSMAQA AARFALSLVQ 

       250        260        270        280        290        300 
GLSGETVVEC TYVEGDGKYA RFFAQPVRLG KEGVEEILPV GTLSAFEQKA LEDMLPTLRA 

       310 
DIELGEKFVN N 

« Hide

References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000436 Genomic DNA. Translation: ABI25330.1.
RefSeqYP_719267.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I491.
SMRQ0I491. Positions 1-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205914.HS_1055.

Proteomic databases

PRIDEQ0I491.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI25330; ABI25330; HS_1055.
GeneID4240553.
KEGGhso:HS_1055.
PATRIC20282143. VBIHaeSom53361_1104.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213792.
KOK00024.
OrthoDBEOG6091FG.

Enzyme and pathway databases

BioCycHSOM205914:GJ7V-1094-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_HISS1
AccessionPrimary (citable) accession number: Q0I491
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: October 3, 2006
Last modified: May 14, 2014
This is version 59 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