ID   RUTD_ECO44              Reviewed;         270 AA.
AC   D3H122;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 45.
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=EC042_1084;
OS   Escherichia coli O44:H18 (strain 042 / EAEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=216592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=042 / EAEC;
RX   PubMed=20098708; DOI=10.1371/journal.pone.0008801;
RA   Chaudhuri R.R., Sebaihia M., Hobman J.L., Webber M.A., Leyton D.L.,
RA   Goldberg M.D., Cunningham A.F., Scott-Tucker A., Ferguson P.R.,
RA   Thomas C.M., Frankel G., Tang C.M., Dudley E.G., Roberts I.S., Rasko D.A.,
RA   Pallen M.J., Parkhill J., Nataro J.P., Thomson N.R., Henderson I.R.;
RT   "Complete genome sequence and comparative metabolic profiling of the
RT   prototypical enteroaggregative Escherichia coli strain 042.";
RL   PLoS ONE 5:E8801-E8801(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; FN554766; CBG33906.1; -; Genomic_DNA.
DR   RefSeq; WP_000777652.1; NC_017626.1.
DR   AlphaFoldDB; D3H122; -.
DR   SMR; D3H122; -.
DR   ESTHER; ecoli-rutD; RutD.
DR   KEGG; elo:EC042_1084; -.
DR   PATRIC; fig|216592.3.peg.1122; -.
DR   HOGENOM; CLU_020336_50_1_6; -.
DR   OMA; HAMSVTD; -.
DR   Proteomes; UP000001407; 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..270
FT                   /note="Putative carbamate hydrolase RutD"
FT                   /id="PRO_0000402958"
SQ   SEQUENCE   270 AA;  29503 MW;  FD7DF5810D56ABFA CRC64;
     MKLSLSPPPY ADAPVVVLIS GLGGSGSYWL PQLAVLEQEY QVICYDQRGT GNNPDTLEED
     YSIAQMAAEL HQALVAAGIE RYAVVGHALG ALVGMQLALD YPASLTVLVS VNGWLRINAH
     TRRCFQVREQ LLHSGGAQAW VEAQPLFLYP ADWMAARAPR LEAEDALALA HFQGKNNLLR
     RLNALKRADF SRHTDRIRCP VQIICASDDL LVPSACSSEL HAALPDSQKM VMRYGGHACN
     VTDPETFNAL LLNGLASLLH HREAACKELL