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Protein

Probable malonic semialdehyde reductase RutE

Gene

rutE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May reduce toxic product malonic semialdehyde to 3-hydroxypropionic acid, which is excreted. RutE is apparently supplemented by YdfG. Required in vivo, but not in vitro in pyrimidine nitrogen degradation.1 Publication

Catalytic activityi

3-hydroxypropanoate + NADP+ = 3-oxopropanoate + NADPH.

Cofactori

FMNCurated

GO - Molecular functioni

  • 3-hydroxypropionate dehydrogenase (NADP+) activity Source: UniProtKB-HAMAP
  • FMN binding Source: EcoCyc

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • nitrogen utilization Source: UniProtKB
  • pyrimidine nucleobase catabolic process Source: EcoCyc
  • uracil catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN, NADP

Enzyme and pathway databases

BioCyciEcoCyc:G6519-MONOMER.
ECOL316407:JW0993-MONOMER.
MetaCyc:G6519-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable malonic semialdehyde reductase RutE (EC:1.1.1.298)
Gene namesi
Name:rutE
Synonyms:ycdI
Ordered Locus Names:b1008, JW0993
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13855. rutE.

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene lose the ability to utilize pyrimidine nucleosides and bases as the sole source of nitrogen at room temperature.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 196196Probable malonic semialdehyde reductase RutEPRO_0000072729Add
BLAST

Proteomic databases

PaxDbiP75894.

Expressioni

Inductioni

Up-regulated by the nitrogen regulatory protein C (NtrC also called GlnG) and repressed by RutR.2 Publications

Interactioni

Protein-protein interaction databases

STRINGi511145.b1008.

Structurei

3D structure databases

ProteinModelPortaliP75894.
SMRiP75894. Positions 27-186.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108RDT. Bacteria.
COG0778. LUCA.
HOGENOMiHOG000236370.
InParanoidiP75894.
KOiK09019.
OMAiTHNGWLD.
OrthoDBiEOG6F29CC.
PhylomeDBiP75894.

Family and domain databases

Gene3Di3.40.109.10. 1 hit.
HAMAPiMF_01204. Oxidoreductase_RutE_HadB.
InterProiIPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
IPR023936. Nitroreductase_RutE.
[Graphical view]
PfamiPF00881. Nitroreductase. 1 hit.
[Graphical view]
SUPFAMiSSF55469. SSF55469. 1 hit.

Sequencei

Sequence statusi: Complete.

P75894-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEAVSPGAL STLFTDARTH NGWRETPVSD ETLREIYALM KWGPTSANCS
60 70 80 90 100
PARIVFTRTA EGKERLRPAL SSGNLQKTLT APVTAIVAWD SEFYERLPLL
110 120 130 140 150
FPHGDARSWF TSSPQLAEET AFRNSSMQAA YLIVACRALG LDTGPMSGFD
160 170 180 190
RQHVDDAFFT GSTLKSNLLI NIGYGDSSKL YARLPRLSFE EACGLL
Length:196
Mass (Da):21,570
Last modified:February 1, 1997 - v1
Checksum:iA28A2B10CEB07FFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74093.1.
AP009048 Genomic DNA. Translation: BAA35775.1.
PIRiF64842.
RefSeqiNP_415528.1. NC_000913.3.
WP_001001176.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74093; AAC74093; b1008.
BAA35775; BAA35775; BAA35775.
GeneIDi946591.
KEGGiecj:JW0993.
eco:b1008.
PATRICi32117245. VBIEscCol129921_1046.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74093.1.
AP009048 Genomic DNA. Translation: BAA35775.1.
PIRiF64842.
RefSeqiNP_415528.1. NC_000913.3.
WP_001001176.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP75894.
SMRiP75894. Positions 27-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi511145.b1008.

Proteomic databases

PaxDbiP75894.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74093; AAC74093; b1008.
BAA35775; BAA35775; BAA35775.
GeneIDi946591.
KEGGiecj:JW0993.
eco:b1008.
PATRICi32117245. VBIEscCol129921_1046.

Organism-specific databases

EchoBASEiEB3615.
EcoGeneiEG13855. rutE.

Phylogenomic databases

eggNOGiENOG4108RDT. Bacteria.
COG0778. LUCA.
HOGENOMiHOG000236370.
InParanoidiP75894.
KOiK09019.
OMAiTHNGWLD.
OrthoDBiEOG6F29CC.
PhylomeDBiP75894.

Enzyme and pathway databases

BioCyciEcoCyc:G6519-MONOMER.
ECOL316407:JW0993-MONOMER.
MetaCyc:G6519-MONOMER.

Miscellaneous databases

PROiP75894.

Family and domain databases

Gene3Di3.40.109.10. 1 hit.
HAMAPiMF_01204. Oxidoreductase_RutE_HadB.
InterProiIPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
IPR023936. Nitroreductase_RutE.
[Graphical view]
PfamiPF00881. Nitroreductase. 1 hit.
[Graphical view]
SUPFAMiSSF55469. SSF55469. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Nitrogen regulatory protein C-controlled genes of Escherichia coli: scavenging as a defense against nitrogen limitation."
    Zimmer D.P., Soupene E., Lee H.L., Wendisch V.F., Khodursky A.B., Peter B.J., Bender R.A., Kustu S.
    Proc. Natl. Acad. Sci. U.S.A. 97:14674-14679(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. Cited for: FUNCTION IN PYRIMIDINE CATABOLISM, DISRUPTION PHENOTYPE, NOMENCLATURE.
    Strain: K12 / MG1655 / ATCC 47076.
  6. "RutR is the uracil/thymine-sensing master regulator of a set of genes for synthesis and degradation of pyrimidines."
    Shimada T., Hirao K., Kori A., Yamamoto K., Ishihama A.
    Mol. Microbiol. 66:744-757(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. "The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problems."
    Kim K.S., Pelton J.G., Inwood W.B., Andersen U., Kustu S., Wemmer D.E.
    J. Bacteriol. 192:4089-4102(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiRUTE_ECOLI
AccessioniPrimary (citable) accession number: P75894
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: February 1, 1997
Last modified: November 11, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The Rut pathway degrades exogenous pyrimidines as the sole nitrogen source at room temperature but not at 37 degrees Celsius, a restriction that is apparently a consequence of an inadequate ability to remove toxic malonic semialdehyde at the higher temperature (RutE/YdfG function).

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.