ID   RUTD_ECOS5              Reviewed;         266 AA.
AC   D2NGI6;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 51.
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=ECSF_0915;
OS   Escherichia coli O150:H5 (strain SE15).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=431946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE15;
RX   PubMed=20008064; DOI=10.1128/jb.01543-09;
RA   Toh H., Oshima K., Toyoda A., Ogura Y., Ooka T., Sasamoto H., Park S.H.,
RA   Iyoda S., Kurokawa K., Morita H., Itoh K., Taylor T.D., Hayashi T.,
RA   Hattori M.;
RT   "Complete genome sequence of the wild-type commensal Escherichia coli
RT   strain SE15, belonging to phylogenetic group B2.";
RL   J. Bacteriol. 192:1165-1166(2010).
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; AP009378; BAI54455.1; -; Genomic_DNA.
DR   RefSeq; WP_001295944.1; NC_013654.1.
DR   AlphaFoldDB; D2NGI6; -.
DR   SMR; D2NGI6; -.
DR   ESTHER; ecoli-rutD; RutD.
DR   KEGG; ese:ECSF_0915; -.
DR   PATRIC; fig|431946.3.peg.959; -.
DR   HOGENOM; CLU_020336_50_1_6; -.
DR   OMA; HAMSVTD; -.
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;
KW   Hydrolase.
FT   CHAIN           1..266
FT                   /note="Putative carbamate hydrolase RutD"
FT                   /id="PRO_0000402951"
SQ   SEQUENCE   266 AA;  28924 MW;  E7D2D9F36129D3AC CRC64;
     MKLSLSPPPY ADAPVVVLIS GLGGSGSYWL PQLAVLDQEY QVVCYDQRGT GNNPDTLAED
     YSIAQMAAEL HQALVAAGIE RYAVVGHALG ALVGMQLALD YPASVTVLVS VNGWLRINTH
     TRRCFQVREQ LLHSGGAQAW VEAQPLFLYP ADWMAARAPR LEAEDALALA HFQGKNNLLR
     RLNALKRADF SHHADRIRCP VQIICASDDL LVPTACSSEL HAALPDSQKM VMRYGGHACN
     VTDPETFNAL LLNGLASLLH HREAAL