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

Q393V1 (MDH_BURS3) 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:Bcep18194_B2154
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier482957 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_01517

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_01517

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01517

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 2 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

Initiator methionine11Removed By similarity
Chain2 – 328327Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000294381

Regions

Nucleotide binding12 – 187NAD By similarity
Nucleotide binding130 – 1323NAD By similarity

Sites

Active site1881Proton acceptor By similarity
Binding site931Substrate By similarity
Binding site991Substrate By similarity
Binding site1061NAD By similarity
Binding site1131NAD By similarity
Binding site1321Substrate By similarity
Binding site1631Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q393V1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: A43D956A12C1FE86

FASTA32835,131
        10         20         30         40         50         60 
MAKPAKRVAV TGAAGQIAYS LLFRIANGDL LGKDQPVILQ LLDLPQAQGA VKGVVMELDD 

        70         80         90        100        110        120 
CAFPLLSGVV ITDDPKVAFK DADVALLVGA RPRSKGMERK DLLSANAEIF TVQGAALNEV 

       130        140        150        160        170        180 
ASRDVKVLVV GNPANTNAYI AMKSAPDLPK KNFTAMLRLD HNRALSQLAA KSGKPVASIE 

       190        200        210        220        230        240 
KLAVWGNHSP TMYPDFRFAT AEGESLLKLI NDDVWNRDTF IPTVGKRGAA IIEARGLSSA 

       250        260        270        280        290        300 
ASAANAAIDH VRDWVLGTNG KWVTMGIPSD GSYGIPEDII YGVPVVCENG EYKRIEGLEI 

       310        320 
DAFSREKMDG TLAELLEERD GVAHLLKN 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia sp. 383."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 383.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000152 Genomic DNA. Translation: ABB12265.1.
RefSeqYP_372909.1. NC_007511.1.

3D structure databases

ProteinModelPortalQ393V1.
SMRQ393V1. Positions 3-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269483.Bcep18194_B2154.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB12265; ABB12265; Bcep18194_B2154.
GeneID3753919.
KEGGbur:Bcep18194_B2154.
PATRIC19295211. VBIBurSp120713_6967.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMANCLIASK.
OrthoDBEOG6PP9Q2.
ProtClustDBPRK05442.

Enzyme and pathway databases

BioCycBSP269483:GHLS-5573-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_01517. Malate_dehydrog_2.
InterProIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR23382. PTHR23382. 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.
TIGRFAMsTIGR01759. MalateDH-SF1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMDH_BURS3
AccessionPrimary (citable) accession number: Q393V1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: November 22, 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