UniProtKB - P75895 (RUTD_ECOLI)
Protein
Putative aminoacrylate hydrolase RutD
Gene
rutD
Organism
Escherichia coli (strain K12)
Status
Functioni
May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation.1 Publication
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).
Catalytic activityi
GO - Molecular functioni
- hydrolase activity Source: GO_Central
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides Source: InterPro
GO - Biological processi
- nitrogen utilization Source: UniProtKB
- pyrimidine nucleobase catabolic process Source: EcoCyc
- uracil catabolic process Source: UniProtKB
Keywordsi
Molecular function | Hydrolase |
Enzyme and pathway databases
BioCyci | EcoCyc:G6520-MONOMER |
Protein family/group databases
ESTHERi | ecoli-rutD, RutD |
Names & Taxonomyi
Protein namesi | Recommended name: Putative aminoacrylate hydrolase RutD (EC:3.5.1.-)Alternative name(s): Aminohydrolase |
Gene namesi | Name:rutD Synonyms:ycdJ Ordered Locus Names:b1009, JW0994 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
Cells lacking this gene form less than the normal amount of malonic semialdehyde because a portion of the 3-carbon intermediate is diverted out of the Rut pathway.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000168800 | 1 – 266 | Putative aminoacrylate hydrolase RutDAdd BLAST | 266 |
Proteomic databases
PaxDbi | P75895 |
PRIDEi | P75895 |
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
BioGRIDi | 4262210, 24 interactors |
STRINGi | 511145.b1009 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 14 – 115 | AB hydrolase-1Sequence analysisAdd BLAST | 102 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG2021, Bacteria |
HOGENOMi | CLU_020336_50_1_6 |
InParanoidi | P75895 |
PhylomeDBi | P75895 |
Family and domain databases
Gene3Di | 3.40.50.1820, 1 hit |
HAMAPi | MF_00832, RutD, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR000073, AB_hydrolase_1 IPR019913, Pyrimidine_utilisation_RutD |
Pfami | View protein in Pfam PF12697, Abhydrolase_6, 1 hit |
PRINTSi | PR00111, ABHYDROLASE |
SUPFAMi | SSF53474, SSF53474, 1 hit |
TIGRFAMsi | TIGR03611, RutD, 1 hit |
i Sequence
Sequence statusi: Complete.
P75895-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKLSLSPPPY ADAPVVVLIS GLGGSGSYWL PQLAVLEQEY QVVCYDQRGT
60 70 80 90 100
GNNPDTLAED YSIAQMAAEL HQALVAAGIE HYAVVGHALG ALVGMQLALD
110 120 130 140 150
YPASVTVLIS VNGWLRINAH TRRCFQVRER LLYSGGAQAW VEAQPLFLYP
160 170 180 190 200
ADWMAARAPR LEAEDALALA HFQGKNNLLR RLNALKRADF SHHADRIRCP
210 220 230 240 250
VQIICASDDL LVPTACSSEL HAALPDSQKM VMPYGGHACN VTDPETFNAL
260
LLNGLASLLH HREAAL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC74094.1 AP009048 Genomic DNA Translation: BAA35776.1 |
PIRi | G64842 |
RefSeqi | NP_415529.1, NC_000913.3 WP_000777653.1, NZ_SSZK01000002.1 |
Genome annotation databases
EnsemblBacteriai | AAC74094; AAC74094; b1009 BAA35776; BAA35776; BAA35776 |
GeneIDi | 57731800 946586 |
KEGGi | ecj:JW0994 eco:b1009 |
PATRICi | fig|1411691.4.peg.1262 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC74094.1 AP009048 Genomic DNA Translation: BAA35776.1 |
PIRi | G64842 |
RefSeqi | NP_415529.1, NC_000913.3 WP_000777653.1, NZ_SSZK01000002.1 |
3D structure databases
SMRi | P75895 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4262210, 24 interactors |
STRINGi | 511145.b1009 |
Protein family/group databases
ESTHERi | ecoli-rutD, RutD |
Proteomic databases
PaxDbi | P75895 |
PRIDEi | P75895 |
Genome annotation databases
EnsemblBacteriai | AAC74094; AAC74094; b1009 BAA35776; BAA35776; BAA35776 |
GeneIDi | 57731800 946586 |
KEGGi | ecj:JW0994 eco:b1009 |
PATRICi | fig|1411691.4.peg.1262 |
Organism-specific databases
EchoBASEi | EB3616 |
Phylogenomic databases
eggNOGi | COG2021, Bacteria |
HOGENOMi | CLU_020336_50_1_6 |
InParanoidi | P75895 |
PhylomeDBi | P75895 |
Enzyme and pathway databases
BioCyci | EcoCyc:G6520-MONOMER |
Miscellaneous databases
PROi | PR:P75895 |
Family and domain databases
Gene3Di | 3.40.50.1820, 1 hit |
HAMAPi | MF_00832, RutD, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR000073, AB_hydrolase_1 IPR019913, Pyrimidine_utilisation_RutD |
Pfami | View protein in Pfam PF12697, Abhydrolase_6, 1 hit |
PRINTSi | PR00111, ABHYDROLASE |
SUPFAMi | SSF53474, SSF53474, 1 hit |
TIGRFAMsi | TIGR03611, RutD, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RUTD_ECOLI | |
Accessioni | P75895Primary (citable) accession number: P75895 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2002 |
Last sequence update: | February 1, 1997 | |
Last modified: | February 10, 2021 | |
This is version 133 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families