ID   RUTD_CAUVN              Reviewed;         269 AA.
AC   B8H1Q3;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=CCNA_02887;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(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; CP001340; ACL96352.1; -; Genomic_DNA.
DR   RefSeq; WP_010920638.1; NC_011916.1.
DR   RefSeq; YP_002518260.1; NC_011916.1.
DR   AlphaFoldDB; B8H1Q3; -.
DR   SMR; B8H1Q3; -.
DR   EnsemblBacteria; ACL96352; ACL96352; CCNA_02887.
DR   GeneID; 7331317; -.
DR   KEGG; ccs:CCNA_02887; -.
DR   PATRIC; fig|565050.3.peg.2817; -.
DR   HOGENOM; CLU_020336_50_1_5; -.
DR   OMA; HAMSVTD; -.
DR   OrthoDB; 1196738at2; -.
DR   PhylomeDB; B8H1Q3; -.
DR   Proteomes; UP000001364; 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; Reference proteome.
FT   CHAIN           1..269
FT                   /note="Putative carbamate hydrolase RutD"
FT                   /id="PRO_0000402929"
FT   DOMAIN          26..144
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00832"
SQ   SEQUENCE   269 AA;  29553 MW;  6822E8086D0ADE0D CRC64;
     MRRMTIGTVD GLHYELHGGP IAGREVVLLS SGLGGSGAFW APQMQALTQR WPVVTYDHRG
     TGRSVRELPP RYTLAHMADD MVKVMDALGL AKAHVVGHAA GGNAGLQLAL DHPDRLAKLV
     VVNGWSRPDP HIRRCFDTRL HLLNDTGPEA YVHAQPIFLY PADWISRNHT RLMAEEAHHV
     AAFPPREVML ARINALLAFD IDARLEDITH RVLISASADD MLVPMSCSQR LAGRLPNADF
     QQVAWGGHGF TVTDPETFNE ALVSFLEGA