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A5UIX3 (MDH_HAEIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:CGSHiGG_09775
OrganismHaemophilus influenzae (strain PittGG) [Complete proteome] [HAMAP]
Taxonomic identifier374931 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

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_1000068590

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
A5UIX3 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 92F655945AD81453

FASTA31132,541
        10         20         30         40         50         60 
MKVAVLGAAG GIGQALALLL KLQLPAGTDL ALYDIAPVTP GVAVDVSHIP TAVNVKGFSG 

        70         80         90        100        110        120 
EDPTPALEGA DVVLISAGVA RKPGMDRSDL FNINAGIVRG LIEKVAITCP KACVGIITNP 

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

       190        200        210        220        230        240 
TILPLLSQVQ YAKWNEEEIE PLTKRIQNAG TEVVNAKAGG GSATLSMAQA AARFARSLVK 

       250        260        270        280        290        300 
GLSGETVVEC TYVEGDGKYA RFFSQPVRLG KEGVEEILPI GPLSNFEQQA LENMLPTLRA 

       310 
DIELGEKFIN G 

« Hide

References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PittGG.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000672 Genomic DNA. Translation: ABR00729.1.
RefSeqYP_001293112.1. NC_009567.1.

3D structure databases

ProteinModelPortalA5UIX3.
SMRA5UIX3. Positions 1-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374931.CGSHiGG_09775.

Proteomic databases

PRIDEA5UIX3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR00729; ABR00729; CGSHiGG_09775.
GeneID5227776.
KEGGhiq:CGSHiGG_09775.
PATRIC20188262. VBIHaeInf102487_1975.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213792.
KOK00024.
OMAFKARGVY.
OrthoDBEOG6091FG.
ProtClustDBPRK05086.

Enzyme and pathway databases

BioCycHINF374931:GJA4-1695-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_HAEIG
AccessionPrimary (citable) accession number: A5UIX3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 10, 2007
Last modified: February 19, 2014
This is version 49 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