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Protein

D-malate dehydrogenase [decarboxylating]

Gene

dmlA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD+-dependent oxidative decarboxylation of D-malate into pyruvate. Is essential for aerobic growth on D-malate as the sole carbon source. But is not required for anaerobic D-malate utilization, although DmlA is expressed and active in those conditions. Appears to be not able to use L-tartrate as a substrate for dehydrogenation instead of D-malate.1 Publication

Catalytic activityi

(R)-malate + NAD+ = pyruvate + CO2 + NADH.2 Publications

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 1 Mg2+ or Mn2+ ion per subunit.By similarity

GO - Molecular functioni

  • 3-isopropylmalate dehydrogenase activity Source: EcoCyc
  • D-malate dehydrogenase (decarboxylating) activity Source: UniProtKB
  • magnesium ion binding Source: EcoCyc
  • NAD binding Source: EcoCyc
  • tartrate dehydrogenase activity Source: EcoCyc

GO - Biological processi

  • malate metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Magnesium, Manganese, NAD

Enzyme and pathway databases

BioCyciEcoCyc:G6986-MONOMER.
ECOL316407:JW1789-MONOMER.
MetaCyc:G6986-MONOMER.
BRENDAi1.1.1.83. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
D-malate dehydrogenase [decarboxylating] (EC:1.1.1.83)
Alternative name(s):
D-malate degradation protein A
D-malate oxidase
Gene namesi
Name:dmlA
Synonyms:yeaU
Ordered Locus Names:b1800, JW1789
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13507. dmlA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Deletion of dmlA inhibits aerobic growth on D-malate but does not impair slow anaerobic growth on D-malate.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000838181 – 361D-malate dehydrogenase [decarboxylating]Add BLAST361

Proteomic databases

PaxDbiP76251.
PRIDEiP76251.

Expressioni

Inductioni

By the transcriptional regulator DmlR in the presence of D-malate or L- or meso-tartrate, under aerobic conditions. Is not induced by L-malate, D-tartrate or succinate. Is also induced at high levels under anaerobic conditions in the presence of D-malate and its expression is more than 5-fold greater than the one under aerobic conditions. Repressed by glucose or nitrate under anaerobic conditions. During aerobic growth, appears to be repressed by the DcuS-DcuR two-component system, and is not repressed by glucose.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi4260335. 13 interactors.
DIPiDIP-11800N.
IntActiP76251. 3 interactors.
MINTiMINT-1273575.
STRINGi511145.b1800.

Structurei

3D structure databases

ProteinModelPortaliP76251.
SMRiP76251.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C0C. Bacteria.
COG0473. LUCA.
HOGENOMiHOG000021111.
InParanoidiP76251.
KOiK07246.
OMAiWGFDLSF.
PhylomeDBiP76251.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
IPR011829. TTC_DH.
[Graphical view]
PANTHERiPTHR11835. PTHR11835. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
SMARTiSM01329. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02089. TTC. 1 hit.
PROSITEiPS00470. IDH_IMDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P76251-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKTMRIAAI PGDGIGKEVL PEGIRVLQAA AERWGFALSF EQMEWASCEY
60 70 80 90 100
YSHHGKMMPD DWHEQLSRFD AIYFGAVGWP DTVPDHISLW GSLLKFRREF
110 120 130 140 150
DQYVNLRPVR LFPGVPCPLA GKQPGDIDFY VVRENTEGEY SSLGGRVNEG
160 170 180 190 200
TEHEVVIQES VFTRRGVDRI LRYAFELAQS RPRKTLTSAT KSNGLAISMP
210 220 230 240 250
YWDERVEAMA ENYPEIRWDK QHIDILCARF VMQPERFDVV VASNLFGDIL
260 270 280 290 300
SDLGPACTGT IGIAPSANLN PERTFPSLFE PVHGSAPDIY GKNIANPIAT
310 320 330 340 350
IWAGAMMLDF LGNGDERFQQ AHNGILAAIE EVIAHGPKTP DMKGNATTPQ
360
VADAICKIIL R
Length:361
Mass (Da):40,315
Last modified:February 1, 1997 - v1
Checksum:i6D77B609729925D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74870.1.
AP009048 Genomic DNA. Translation: BAA15595.1.
PIRiH64940.
RefSeqiNP_416314.1. NC_000913.3.
WP_000978494.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74870; AAC74870; b1800.
BAA15595; BAA15595; BAA15595.
GeneIDi946319.
KEGGiecj:JW1789.
eco:b1800.
PATRICi32118917. VBIEscCol129921_1876.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74870.1.
AP009048 Genomic DNA. Translation: BAA15595.1.
PIRiH64940.
RefSeqiNP_416314.1. NC_000913.3.
WP_000978494.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP76251.
SMRiP76251.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260335. 13 interactors.
DIPiDIP-11800N.
IntActiP76251. 3 interactors.
MINTiMINT-1273575.
STRINGi511145.b1800.

Proteomic databases

PaxDbiP76251.
PRIDEiP76251.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74870; AAC74870; b1800.
BAA15595; BAA15595; BAA15595.
GeneIDi946319.
KEGGiecj:JW1789.
eco:b1800.
PATRICi32118917. VBIEscCol129921_1876.

Organism-specific databases

EchoBASEiEB3280.
EcoGeneiEG13507. dmlA.

Phylogenomic databases

eggNOGiENOG4105C0C. Bacteria.
COG0473. LUCA.
HOGENOMiHOG000021111.
InParanoidiP76251.
KOiK07246.
OMAiWGFDLSF.
PhylomeDBiP76251.

Enzyme and pathway databases

BioCyciEcoCyc:G6986-MONOMER.
ECOL316407:JW1789-MONOMER.
MetaCyc:G6986-MONOMER.
BRENDAi1.1.1.83. 2026.

Miscellaneous databases

PROiP76251.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
IPR011829. TTC_DH.
[Graphical view]
PANTHERiPTHR11835. PTHR11835. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
SMARTiSM01329. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02089. TTC. 1 hit.
PROSITEiPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDMLA_ECOLI
AccessioniPrimary (citable) accession number: P76251
Secondary accession number(s): O08474, O08475
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: November 2, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Aerobic growth on D-malate requires, in addition to DmlA, the presence of the aerobic C4-dicarboxylate transporter DctA, for D-malate uptake. Meso-tartrate or L-tartrate are not able to support aerobic growth. Slow anaerobic growth on D-malate is observed only when glycerol is also provided as an electron donor, and D-malate is used in fumarate respiration, so is not dependent on DmlA.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.