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A0LFF8

- MDH_SYNFM

UniProt

A0LFF8 - MDH_SYNFM

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Protein

Malate dehydrogenase

Gene
mdh, Sfum_0460
Organism
Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the reversible oxidation of malate to oxaloacetate. Catalyzes the reduction of oxaloacetate more efficiently than the oxidation of malate.1 Publication

Catalytic activityi

(S)-malate + NAD+ = oxaloacetate + NADH.1 Publication

Enzyme regulationi

Substrate inhibition is observed at high concentrations of oxaloacetate.1 Publication

Kineticsi

  1. KM=50 µM for oxaloacetate (at 37 degrees Celsius and pH 7.5)1 Publication
  2. KM=30 µM for NADH (at 37 degrees Celsius and pH 7.5)
  3. KM=4 mM for L-malate (at 37 degrees Celsius and pH 9.0)
  4. KM=1.1 mM for NAD (at 37 degrees Celsius and pH 9.0)

pH dependencei

Optimum pH is 8.5 with oxaloacetate as substrate.

Temperature dependencei

Optimum temperature is 60 degrees Celsius with oxaloacetate as substrate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951Substrate By similarity
Binding sitei101 – 1011Substrate By similarity
Binding sitei108 – 1081NAD By similarity
Binding sitei115 – 1151NAD By similarity
Binding sitei134 – 1341Substrate By similarity
Binding sitei165 – 1651Substrate By similarity
Active sitei190 – 1901Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 187NAD By similarity
Nucleotide bindingi132 – 1343NAD By similarity

GO - Molecular functioni

  1. L-malate dehydrogenase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. malate metabolic process Source: InterPro
  3. tricarboxylic acid cycle Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciSFUM335543:GH6P-468-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase (EC:1.1.1.37)
Gene namesi
Name:mdh
Ordered Locus Names:Sfum_0460
OrganismiSyntrophobacter fumaroxidans (strain DSM 10017 / MPOB)
Taxonomic identifieri335543 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophobacteraceaeSyntrophobacter
ProteomesiUP000001784: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 329328Malate dehydrogenaseUniRule annotationPRO_0000292376Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi335543.Sfum_0460.

Structurei

3D structure databases

ProteinModelPortaliA0LFF8.
SMRiA0LFF8. Positions 3-327.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0039.
HOGENOMiHOG000220953.
KOiK00024.
OMAiCALRDEV.
OrthoDBiEOG6PP9Q2.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2.
InterProiIPR001557. 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]
PANTHERiPTHR23382. PTHR23382. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A0LFF8-1 [UniParc]FASTAAdd to Basket

« Hide

MAKKPVRVTV TGAAGQIGYA LLFRVASGQM LGPDQPIILQ MLELPIDKVQ    50
AALKGVMMEL EDCAFPLLAD MIGTGDPKVA FKDSDYALLV GARPRGPGME 100
RKDLLLENAK IFIEQGKAMN AVASRDIRVI VVGNPANTNA WIAMKSAPDL 150
PKGNFTAMLR LDHNRAKSQL ATRTGKPVAS VEKMIVWGNH SPTMYPDIRF 200
CTVDGQPAVK LVNDEAWYRN EYIPKVGKRG AAIIEARGLS SAASAANAAI 250
DHMHDWALGT NGKWVTMGLP SDGSYGIPEG TMYGVPVTCT PGKYERVKGL 300
EIDAFSREKM DFTLKELTEE QAGVKEMVK 329
Length:329
Mass (Da):35,690
Last modified:December 12, 2006 - v1
Checksum:i1BE66E683446BE07
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000478 Genomic DNA. Translation: ABK16160.1.
RefSeqiYP_844595.1. NC_008554.1.

Genome annotation databases

EnsemblBacteriaiABK16160; ABK16160; Sfum_0460.
GeneIDi4460269.
KEGGisfu:Sfum_0460.
PATRICi23845877. VBISynFum78438_0536.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000478 Genomic DNA. Translation: ABK16160.1 .
RefSeqi YP_844595.1. NC_008554.1.

3D structure databases

ProteinModelPortali A0LFF8.
SMRi A0LFF8. Positions 3-327.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 335543.Sfum_0460.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK16160 ; ABK16160 ; Sfum_0460 .
GeneIDi 4460269.
KEGGi sfu:Sfum_0460.
PATRICi 23845877. VBISynFum78438_0536.

Phylogenomic databases

eggNOGi COG0039.
HOGENOMi HOG000220953.
KOi K00024.
OMAi CALRDEV.
OrthoDBi EOG6PP9Q2.

Enzyme and pathway databases

BioCyci SFUM335543:GH6P-468-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPi MF_01517. Malate_dehydrog_2.
InterProi IPR001557. 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 ]
PANTHERi PTHR23382. PTHR23382. 1 hit.
Pfami PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMi SSF56327. SSF56327. 1 hit.
TIGRFAMsi TIGR01759. MalateDH-SF1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiMDH_SYNFM
AccessioniPrimary (citable) accession number: A0LFF8
Secondary accession number(s): P80648
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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