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

A7IBL9 (MDH_XANP2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:Xaut_0153
OrganismXanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) [Complete proteome] [HAMAP]
Taxonomic identifier78245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeXanthobacter

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_00487

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_00487

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 3 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 – 321321Malate dehydrogenase HAMAP-Rule MF_00487
PRO_1000126151

Regions

Nucleotide binding10 – 156NAD By similarity
Nucleotide binding119 – 1213NAD By similarity

Sites

Active site1761Proton acceptor By similarity
Binding site341NAD By similarity
Binding site831Substrate By similarity
Binding site891Substrate By similarity
Binding site961NAD By similarity
Binding site1211Substrate By similarity
Binding site1521Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A7IBL9 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: E6DAFF8A89026D1B

FASTA32133,664
        10         20         30         40         50         60 
MARNKIALIG AGQIGGTLAL LAGMKALGDI VLFDVAEGVP EGKALDLAEL TPVEGFDAAY 

        70         80         90        100        110        120 
AGASSYDAIS GADVVIVTAG VARKPGMSRD DLLAINLKVM EQVGAGIRKY APDAFVICIT 

       130        140        150        160        170        180 
NPLDAMVWAL QRSSGLPPEK VVGMAGVLDS ARLRYFLAEE FGVSVEDVTA FVMGGHGDTM 

       190        200        210        220        230        240 
VPLVRYSTVG GIPVPDLIRM GWTSEERIAA IVQRTRDGGA EIVNLLKSGS AFYAPAASAI 

       250        260        270        280        290        300 
AMAESYLRDK KRVLPVAALL DGEYGLRDIY VGVPAVIGAR GVERIVEVEL DRSERAMFDR 

       310        320 
SVAAVEGLVE ACLKIAPGLG K 

« Hide

References

[1]"Complete sequence of chromosome of Xanthobacter autotrophicus Py2."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Brainard J., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1158 / Py2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000781 Genomic DNA. Translation: ABS65412.1.
RefSeqYP_001415069.1. NC_009720.1.

3D structure databases

ProteinModelPortalA7IBL9.
SMRA7IBL9. Positions 3-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING78245.Xaut_0153.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS65412; ABS65412; Xaut_0153.
GeneID5422091.
KEGGxau:Xaut_0153.
PATRIC24042266. VBIXanAut29526_0444.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMADANIVEC.
OrthoDBEOG6091FG.
ProtClustDBPRK06223.

Enzyme and pathway databases

BioCycXAUT78245:GHS6-153-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_00487. Malate_dehydrog_3.
InterProIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR011275. Malate_DH_type3.
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.
PRINTSPR00086. LLDHDRGNASE.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01763. MalateDH_bact. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMDH_XANP2
AccessionPrimary (citable) accession number: A7IBL9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 51 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