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Q5U907 (MDH_ACTSZ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 68. 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:Asuc_1612
OrganismActinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]
Taxonomic identifier339671 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus

Protein attributes

Sequence length312 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 – 312312Malate dehydrogenase HAMAP-Rule MF_01516
PRO_0000113299

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
Q5U907 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 029DEF60E6D2106A

FASTA31233,115
        10         20         30         40         50         60 
MKVTLLGASG GIGQPLSLLL KLHLPAESDL SLYDVAPVTP GVAKDISHIP TSVEVEGFGG 

        70         80         90        100        110        120 
DDPSEALKGA DIVLICAGVA RKPGMTRADL FNVNAGIIQN LVEKVAQVCP QACVCIITNP 

       130        140        150        160        170        180 
VNSIIPIAAE VLKKAGVYDK RKLFGITTLD TIRSEKFIVQ AKNIEINRND ISVIGGHSGV 

       190        200        210        220        230        240 
TILPLLSQIP HVEFTEQELK DLTHRIQNAG TEVVEAKAGA GSATLSMAYA AMRFVVSMAR 

       250        260        270        280        290        300 
ALNGEVITEC AYIEGDGKFA RFFAQPVRLG KNGVEEILPL GTLSAFEQQA LEAMLPTLQT 

       310 
DIDNGVKFVT GE 

« Hide

References

« Hide 'large scale' references
[1]"Actinobacillus succinogenes mdh gene cloning and recombinant enzyme characterization."
Laivenieks M., Vieille C., Zeikus J.G.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Actinobacillus succinogenes 130Z."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 55618 / 130Z.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY773261 Genomic DNA. Translation: AAV41054.1.
CP000746 Genomic DNA. Translation: ABR74966.1.
RefSeqYP_001344901.1. NC_009655.1.

3D structure databases

ProteinModelPortalQ5U907.
SMRQ5U907. Positions 1-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING339671.Asuc_1612.

Proteomic databases

PRIDEQ5U907.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR74966; ABR74966; Asuc_1612.
GeneID5348645.
KEGGasu:Asuc_1612.
PATRIC20761606. VBIActSuc117883_1677.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213792.
KOK00024.
OMAVEVKGFA.
OrthoDBEOG6091FG.

Enzyme and pathway databases

BioCycASUC339671:GHDX-1682-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_ACTSZ
AccessionPrimary (citable) accession number: Q5U907
Secondary accession number(s): A6VPR9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 7, 2004
Last modified: June 11, 2014
This is version 68 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