(data stored in ACNUC7421 zone)

HOGENOM: ECO8A_1_PE1012

ID   ECO8A_1_PE1012                       STANDARD;      PRT;   266 AA.
AC   ECO8A_1_PE1012; B7M8Z4;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Putative aminoacrylate hydrolase RutD; EC=3.5.1 -;AltName:
DE   Full=Aminohydrolase; (ECO8A_1.PE1012).
GN   Name=rutD; OrderedLocusNames=ECIAI1_1054;
OS   ESCHERICHIA COLI IAI1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECO8A_1.PE1012.
CC       Escherichia coli IAI1, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:RUTD_ECO8A
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 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: (Z)-3-aminoacrylate + H(2)O = malonate
CC       semialdehyde + NH(3).
CC   -!- INDUCTION: Up-regulated by the nitrogen regulatory protein C (NtrC
CC       also called GlnG) and repressed by RutR (Potential).
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Hydrolase
CC       RutD family.
CC   -!- GENE_FAMILY: HOG000028072 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B7M8Z4; -.
DR   EMBL; CU928160; CAQ97918.1; -; Genomic_DNA.
DR   RefSeq; YP_002386511.1; NC_011741.1.
DR   ProteinModelPortal; B7M8Z4; -.
DR   STRING; B7M8Z4; -.
DR   EnsemblBacteria; EBESCT00000132936; EBESCP00000124367; EBESCG00000131786.
DR   GeneID; 7124640; -.
DR   GenomeReviews; CU928160_GR; ECIAI1_1054.
DR   GeneTree; EBGT00050000009729; -.
DR   OMA; LADITTP; -.
DR   ProtClustDB; CLSK879922; -.
DR   BioCyc; ECOL585034:ECIAI1_1054-MON; -.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InteDR   HAMAP; MF_00832; RutD; 1; -.
DR   HAMAP; MF_00832; RutD; 1; -.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR019913; Pyrimidine_utilisation_RutD.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   TIGRFAMs; TIGR03611; RutD; 1.
DR   HOGENOMDNA; ECO8A_1.PE1012; -.
KW   Complete proteome; Hydrolase.
SQ   SEQUENCE   266 AA;  UNKNOWN MW;  UNKNOWN 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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