ID   RUTD_KLEVT              Reviewed;         266 AA.
AC   D3RKL3;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   25-MAY-2022, entry version 47.
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=Kvar_3344;
OS   Klebsiella variicola (strain At-22).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=640131;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=At-22;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Pinto A.,
RA   Currie C., Woyke T.;
RT   "Complete sequence of Klebsiella variicola At-22.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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; CP001891; ADC59224.1; -; Genomic_DNA.
DR   RefSeq; WP_012968590.1; NC_013850.1.
DR   AlphaFoldDB; D3RKL3; -.
DR   SMR; D3RKL3; -.
DR   GeneID; 56939603; -.
DR   KEGG; kva:Kvar_3344; -.
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; PF00561; Abhydrolase_1; 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_0000402969"
FT   DOMAIN          15..239
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00832"
SQ   SEQUENCE   266 AA;  28262 MW;  BDB86CAA46B4234D CRC64;
     MMRLNIAPAP WPGAPVVVLS AGLGGGGGYW LAQRAALEAQ YQLVSYDHNG TGENAGPLPA
     DYSMATMAQE LLSALQAAGI TRFALVGHAL GALIGLQLAL DRPEAVSALV LVNGWLTLSP
     HTRRCFLVRE RLLHAGGAQA WVEAQPLFLY PAEWMAARLP RLEAEDALAI SHFQGKENLL
     KRLQALKQAD FSRRAAAIAC PTLIVSAADD LLVPASCSRV LQAAIPGSQR VEMPWGGHAC
     NVTDADTFNT ILCDGLAAML PVAREI