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

Q1QQR2 (MDH_NITHX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:Nham_0545
OrganismNitrobacter hamburgensis (strain X14 / DSM 10229) [Complete proteome] [HAMAP]
Taxonomic identifier323097 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter

Protein attributes

Sequence length322 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 – 322322Malate dehydrogenase HAMAP-Rule MF_00487
PRO_1000026479

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
Q1QQR2 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 639C0D40C21F552D

FASTA32234,063
        10         20         30         40         50         60 
MARDKIALIG SGQIGGTLAH LIGLKELGDV VMFDIAEGIP QGKSLDIAQS SPVDGFDAKL 

        70         80         90        100        110        120 
TGANSYEALE GARVCIVTAG IPRKPGMSRD DLLSINLKVM EQVGAGIKKY APDAFVICIT 

       130        140        150        160        170        180 
NPLDAMVWAL QKASGMPAKK VVGMAGVLDS SRFRYFLADE FDVSVEDVTA FVLGGHGDSM 

       190        200        210        220        230        240 
VPLVKYSTVA GIPLPDLVKM GWTSQARIDE IVDRTRNGGA EIVNLLKTGS AFYAPAASAI 

       250        260        270        280        290        300 
AMAESYLRDK KRVLPCAAYL NGEFGVKDMY VGVPVVIGAR GVERIVEIEL AGKDREAFDK 

       310        320 
SVGAVQGLID ACKKIAPDLL GK 

« Hide

References

[1]"Complete sequence of chromosome of Nitrobacter hamburgensis X14."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: X14 / DSM 10229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000319 Genomic DNA. Translation: ABE61435.1.
RefSeqYP_575895.1. NC_007964.1.

3D structure databases

ProteinModelPortalQ1QQR2.
SMRQ1QQR2. Positions 1-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323097.Nham_0545.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE61435; ABE61435; Nham_0545.
GeneID4030837.
KEGGnha:Nham_0545.
PATRIC22688505. VBINitHam61822_1289.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAGANSYEA.
OrthoDBEOG6091FG.
ProtClustDBPRK06223.

Enzyme and pathway databases

BioCycNHAM323097:GHP7-554-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_NITHX
AccessionPrimary (citable) accession number: Q1QQR2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: February 19, 2014
This is version 59 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