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A0LFF8 (MDH_SYNFM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 55. 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:Sfum_0460
OrganismSyntrophobacter fumaroxidans (strain DSM 10017 / MPOB) [Complete proteome] [HAMAP]
Taxonomic identifier335543 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophobacteraceaeSyntrophobacter

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate. Catalyzes the reduction of oxaloacetate more efficiently than the oxidation of malate. Ref.2

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. Ref.2

Enzyme regulation

Substrate inhibition is observed at high concentrations of oxaloacetate. Ref.2

Subunit structure

Homodimer. Ref.2

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 2 family.

Biophysicochemical properties

Kinetic parameters:

KM=50 µM for oxaloacetate (at 37 degrees Celsius and pH 7.5) Ref.2

KM=30 µM for NADH (at 37 degrees Celsius and pH 7.5)

KM=4 mM for L-malate (at 37 degrees Celsius and pH 9.0)

KM=1.1 mM for NAD (at 37 degrees Celsius and pH 9.0)

pH dependence:

Optimum pH is 8.5 with oxaloacetate as substrate.

Temperature dependence:

Optimum temperature is 60 degrees Celsius with oxaloacetate as substrate.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 329328Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000292376

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
A0LFF8 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 1BE66E683446BE07

FASTA32935,690
        10         20         30         40         50         60 
MAKKPVRVTV TGAAGQIGYA LLFRVASGQM LGPDQPIILQ MLELPIDKVQ AALKGVMMEL 

        70         80         90        100        110        120 
EDCAFPLLAD MIGTGDPKVA FKDSDYALLV GARPRGPGME RKDLLLENAK IFIEQGKAMN 

       130        140        150        160        170        180 
AVASRDIRVI VVGNPANTNA WIAMKSAPDL PKGNFTAMLR LDHNRAKSQL ATRTGKPVAS 

       190        200        210        220        230        240 
VEKMIVWGNH SPTMYPDIRF CTVDGQPAVK LVNDEAWYRN EYIPKVGKRG AAIIEARGLS 

       250        260        270        280        290        300 
SAASAANAAI DHMHDWALGT NGKWVTMGLP SDGSYGIPEG TMYGVPVTCT PGKYERVKGL 

       310        320 
EIDAFSREKM DFTLKELTEE QAGVKEMVK 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of Syntrophobacter fumaroxidans MPOB."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Boone D.R. expand/collapse author list , Brockman F., Culley D., Ferry J., Gunsalus R., McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 10017 / MPOB.
[2]"Purification and characterization of malate dehydrogenase from the syntrophic propionate-oxidizing bacterium strain MPOB."
van Kuijk B.L.M., Stams A.J.M.
FEMS Microbiol. Lett. 144:141-144(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-22, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000478 Genomic DNA. Translation: ABK16160.1.
RefSeqYP_844595.1. NC_008554.1.

3D structure databases

ProteinModelPortalA0LFF8.
SMRA0LFF8. Positions 3-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335543.Sfum_0460.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK16160; ABK16160; Sfum_0460.
GeneID4460269.
KEGGsfu:Sfum_0460.
PATRIC23845877. VBISynFum78438_0536.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMACALRDEV.
OrthoDBEOG6PP9Q2.

Enzyme and pathway databases

BioCycSFUM335543:GH6P-468-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_SYNFM
AccessionPrimary (citable) accession number: A0LFF8
Secondary accession number(s): P80648
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: December 12, 2006
Last modified: June 11, 2014
This is version 55 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