ID   RUTD_ENTCC              Reviewed;         266 AA.
AC   D5CE35;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 48.
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=ECL_02625;
OS   Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC
OS   13535 / NCTC 10005 / WDCM 00083 / NCDC 279-56).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=716541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC
RC   279-56;
RX   PubMed=20207761; DOI=10.1128/jb.00067-10;
RA   Ren Y., Ren Y., Zhou Z., Guo X., Li Y., Feng L., Wang L.;
RT   "Complete genome sequence of Enterobacter cloacae subsp. cloacae type
RT   strain ATCC 13047.";
RL   J. Bacteriol. 192:2463-2464(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; CP001918; ADF62168.1; -; Genomic_DNA.
DR   RefSeq; WP_013097196.1; NC_014121.1.
DR   RefSeq; YP_003613117.1; NC_014121.1.
DR   AlphaFoldDB; D5CE35; -.
DR   SMR; D5CE35; -.
DR   STRING; 716541.ECL_02625; -.
DR   EnsemblBacteria; ADF62168; ADF62168; ECL_02625.
DR   KEGG; enc:ECL_02625; -.
DR   PATRIC; fig|716541.4.peg.2798; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020336_50_1_6; -.
DR   OMA; HAMSVTD; -.
DR   Proteomes; UP000002363; 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..266
FT                   /note="Putative carbamate hydrolase RutD"
FT                   /id="PRO_0000402933"
SQ   SEQUENCE   266 AA;  28592 MW;  18A00460CF22786E CRC64;
     MKLSVSPPPF DGAPVVVLIA GLGGGGSYWL PQLAALEQEY QVVCYDQRGT GNNPDTLPEE
     YTLAQMAGEL AQALTAVGIT RYCVVGHALG ALIGLQLALD TPDALKALVC VNGWLTLNAH
     TRRCFQIRER LLHAGGAQAW VEAQPLFLYP ADWMAARAPR LEAEEALALA HFQGKNNLLR
     RLNALKKADF SRHAARMACP VHLICSADDL LVPSVCSSEL QAALPHSHSV VMRQGGHACN
     VTEPETFNTL LLNGLASLLH SHEPAL