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Q2L068 (MDH_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:BAV1180
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length329 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 – 329328Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000294375

Regions

Nucleotide binding12 – 187NAD By similarity
Nucleotide binding132 – 1343NAD By similarity

Sites

Active site1901Proton acceptor By similarity
Binding site951Substrate By similarity
Binding site1011Substrate By similarity
Binding site1081NAD By similarity
Binding site1151NAD By similarity
Binding site1341Substrate By similarity
Binding site1651Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2L068 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: FC0BBE8D7B4E3812

FASTA32935,503
        10         20         30         40         50         60 
MSKPAMRVAV TGAAGQIGYA LLFRIASGEM LGKDQPVILQ LLEIPDEKAQ KALKGVIMEL 

        70         80         90        100        110        120 
EDCAFPLLQE VTAHADPKTA FKDADVALLV GARPRGPGME RKDLLTVNAQ IFTAQGRALN 

       130        140        150        160        170        180 
EVASRNVKVL VVGNPANTNA YIAMKSAPDL PAKNFTAMLR LDHNRALSQL AGKSGKAVAG 

       190        200        210        220        230        240 
IEKLIVWGNH SPTMYPDYRF ATVDGQPLAK LINDEAWNRD TFIPTVGKRG AAIIEARGLS 

       250        260        270        280        290        300 
SAASAANAAI DHVRDWVLGS NGKWVTMGIP SDGSYGIPEG IIYGFPVTTA NGEYTMVKDL 

       310        320 
EVDAFSRERM DFTLKELLEE RDGIKDLLK 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ48788.1.
RefSeqYP_785702.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2L068.
SMRQ2L068. Positions 3-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360910.BAV1180.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6267581.
KEGGbav:BAV1180.
PATRIC21128570. VBIBorAvi43433_1209.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMAAFSQECI.
OrthoDBEOG6PP9Q2.

Enzyme and pathway databases

BioCycBAVI360910:GCKI-1201-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_BORA1
AccessionPrimary (citable) accession number: Q2L068
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: March 7, 2006
Last modified: May 14, 2014
This is version 61 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