ID   RUTD_CAUSK              Reviewed;         268 AA.
AC   B0SW62;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=Caul_3981;
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX   NCBI_TaxID=366602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) 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; CP000927; ABZ73106.1; -; Genomic_DNA.
DR   RefSeq; WP_012287997.1; NC_010338.1.
DR   AlphaFoldDB; B0SW62; -.
DR   SMR; B0SW62; -.
DR   STRING; 366602.Caul_3981; -.
DR   ESTHER; 9caul-q0lxe3; RutD.
DR   EnsemblBacteria; ABZ73106; ABZ73106; Caul_3981.
DR   KEGG; cak:Caul_3981; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_020336_50_1_5; -.
DR   OMA; HAMSVTD; -.
DR   OrthoDB; 1196738at2; -.
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..268
FT                   /note="Putative carbamate hydrolase RutD"
FT                   /id="PRO_0000402931"
FT   DOMAIN          24..243
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00832"
SQ   SEQUENCE   268 AA;  28884 MW;  4FDD3A2A424A2B0A CRC64;
     MQSGTVDGLY HEVHGGPASD RQTVILSAGL GGSGTFWAPQ MQALMSRFRV VLYDHRGTGR
     SARTLTDPHT VAAMGDDIVK LMDALGLERA HVVGHAAGGN AGLALALNHP DRLDKLVVVN
     GWSRPDPHIK RCFDTRLALL NDTGIAAYVH AQPLFLYPAD WLSANNARLE AEEVHHINGF
     PSPDVMRTRI QALLEFDIDE DLETIRCPVL VSASADDMLV PLSCSRRLAE RLPNATLDIA
     PWGGHGFTVT APEAFNAAVL NFLSGEAA