ID   RUTD_ECOL6              Reviewed;         275 AA.
AC   Q8FJ43;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Putative carbamate 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=c1146;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Involved in pyrimidine catabolism. May facilitate the
CC       hydrolysis of carbamate, a reaction that can also occur spontaneously.
CC       {ECO:0000255|HAMAP-Rule:MF_00832}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamate + 2 H(+) = CO2 + NH4(+); Xref=Rhea:RHEA:15649,
CC         ChEBI:CHEBI:13941, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:28938; Evidence={ECO:0000255|HAMAP-Rule:MF_00832};
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Hydrolase RutD
CC       family. {ECO:0000255|HAMAP-Rule:MF_00832}.
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DR   EMBL; AE014075; AAN79614.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8FJ43; -.
DR   SMR; Q8FJ43; -.
DR   STRING; 199310.c1146; -.
DR   ESTHER; ecoli-rutD; RutD.
DR   EnsemblBacteria; AAN79614; AAN79614; c1146.
DR   KEGG; ecc:c1146; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_020336_50_1_6; -.
DR   OMA; HAMSVTD; -.
DR   BioCyc; ECOL199310:C1146-MON; -.
DR   Proteomes; UP000001410; Chromosome.
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   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR03611; RutD; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..275
FT                   /note="Putative carbamate hydrolase RutD"
FT                   /id="PRO_0000402961"
SQ   SEQUENCE   275 AA;  29814 MW;  7066B4CFF3BCED86 CRC64;
     MRISPSETAM KLSLSPPPYA DAPVVVLISG LGGSGSYWLP QLAVLDQEYQ VVCYDQRGTG
     NNPDTLAEDY SIAQMAAELH QALVAAGIER YAVVGHALGA LVGMQLALDY PASVTVLVSV
     NGWLRINAHT RRCFQVREQL LHSGGAQAWV EAQPLFLYPA DWMAARAPRL EAEGALALAH
     FQGKNNLLRR LNALKRADFS RHADRIRCPV QIICASDDLL VPSACSSELH AALPDSQKMV
     MRYGGHACNV TDPETFNALL LNGLASLLHH REAAL