ID   RUTD_CAUST              Reviewed;         267 AA.
AC   D5VGV3;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   25-MAY-2022, entry version 55.
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=Cseg_2080;
OS   Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 /
OS   LMG 17158 / TK0059) (Mycoplana segnis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=509190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 / TK0059;
RX   PubMed=21705585; DOI=10.1128/jb.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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; CP002008; ADG10546.1; -; Genomic_DNA.
DR   RefSeq; WP_013079201.1; NC_014100.1.
DR   AlphaFoldDB; D5VGV3; -.
DR   SMR; D5VGV3; -.
DR   STRING; 509190.Cseg_2080; -.
DR   EnsemblBacteria; ADG10546; ADG10546; Cseg_2080.
DR   KEGG; cse:Cseg_2080; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_020336_50_1_5; -.
DR   OMA; HAMSVTD; -.
DR   OrthoDB; 1196738at2; -.
DR   Proteomes; UP000002629; 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; 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..267
FT                   /note="Putative carbamate hydrolase RutD"
FT                   /id="PRO_0000402930"
FT   DOMAIN          23..139
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00832"
SQ   SEQUENCE   267 AA;  29078 MW;  84C64F027CD4B846 CRC64;
     MTTGTVDGIC YEVHGWPVAG REVVLLSSGL GGSAAFWAPQ MKALTERWPV VTYDHRGTGR
     SVRALPPGPY SVDDMAQDMV KVMDALGLTK AHVVGHAAGG NAGLALALNH PDRLGKLVVV
     NGWSRPDPHI QRCFDTRIHL LNDTGIKAYV HAQPIFLYPA DWISRNHARL MAEEAHHVAG
     FPPREVMLAR INALLAFDID ARLEEIPHRV LVSASADDML VPMSCSQRLA ARLPNADFQQ
     VAWGGHGFTV TDPETFNEGL IKFLEGA