(data stored in ACNUC7421 zone)

SWISSPROT: RUTD_ECO8A

ID   RUTD_ECO8A              Reviewed;         266 AA.
AC   B7M8Z4;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   11-DEC-2019, entry version 51.
DE   RecName: Full=Putative aminoacrylate hydrolase RutD {ECO:0000255|HAMAP-Rule:MF_00832};
DE            EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_00832};
DE   AltName: Full=Aminohydrolase {ECO:0000255|HAMAP-Rule:MF_00832};
GN   Name=rutD {ECO:0000255|HAMAP-Rule:MF_00832}; OrderedLocusNames=ECIAI1_1054;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: May increase the rate of spontaneous hydrolysis of
CC       aminoacrylate to malonic semialdehyde. Required to remove a toxic
CC       intermediate produce in the pyrimidine nitrogen degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_00832}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(Z)-3-aminoacrylate + H(+) + H2O = 3-oxopropanoate + NH4(+);
CC         Xref=Rhea:RHEA:34947, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:33190, ChEBI:CHEBI:59894;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00832};
CC   -!- INDUCTION: Up-regulated by the nitrogen regulatory protein C (NtrC also
CC       called GlnG) and repressed by RutR. {ECO:0000255|HAMAP-Rule:MF_00832}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Hydrolase RutD
CC       family. {ECO:0000255|HAMAP-Rule:MF_00832}.
DR   EMBL; CU928160; CAQ97918.1; -; Genomic_DNA.
DR   RefSeq; WP_001384404.1; NC_011741.1.
DR   SMR; B7M8Z4; -.
DR   ESTHER; ecoli-rutD; RutD.
DR   EnsemblBacteria; CAQ97918; CAQ97918; ECIAI1_1054.
DR   KEGG; ecr:ECIAI1_1054; -.
DR   HOGENOM; HOG000028072; -.
DR   KO; K09023; -.
DR   OMA; HAMSVTD; -.
DR   BioCyc; ECOL585034:ECIAI1_RS05375-MONOMER; -.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0019740; P:nitrogen utilization; IEA:UniProtKB-UniRule.
DR   GO; GO:0006212; P:uracil catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_00832; RutD; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR019913; Pyrimidine_utilisation_RutD.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR03611; RutD; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7M8Z4.
DR   SWISS-2DPAGE; B7M8Z4.
KW   Hydrolase.
FT   CHAIN           1..266
FT                   /note="Putative aminoacrylate hydrolase RutD"
FT                   /id="PRO_0000402964"
FT   DOMAIN          14..115
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   266 AA;  28926 MW;  E155670B0794C140 CRC64;
     MKLSLSPPPY ADAPVVVLIS GLGGSGSYWL PQLAVLEQEY QVVCYDQRGT GNNPDTLAED
     YSIAQMAAEL HQALVAAGIE HYAVVGHALG ALVGMQLALD YPASVTVLIS VNGWLRINAH
     TRRCFQVRER LLYSGGAQAW VEAQPLFLYP ADWMAARVPR LEAEDALALA HFQGKNNLLR
     RLNALKRADF SHHADRIRCP VQIICASDDL LVPTACSSEL HAALPDSQKM VMPYGGHACN
     VTDPETFNAL LLNGLASLLH HREAAL
//

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