ID   RUTD_AGRRK              Reviewed;         262 AA.
AC   B9JLT6;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=Arad_7070;
OS   Agrobacterium radiobacter (strain K84 / ATCC BAA-868).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=311403;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K84 / ATCC BAA-868;
RX   PubMed=19251847; DOI=10.1128/jb.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA   Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA   Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA   Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA   Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
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; CP000629; ACM28650.1; -; Genomic_DNA.
DR   RefSeq; WP_012649156.1; NC_011983.1.
DR   AlphaFoldDB; B9JLT6; -.
DR   SMR; B9JLT6; -.
DR   STRING; 311403.Arad_7070; -.
DR   PRIDE; B9JLT6; -.
DR   EnsemblBacteria; ACM28650; ACM28650; Arad_7070.
DR   KEGG; ara:Arad_7070; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020336_50_1_5; -.
DR   OMA; HAMSVTD; -.
DR   OrthoDB; 1196738at2; -.
DR   Proteomes; UP000001600; Chromosome 2.
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; IPR022742; Hydrolase_4.
DR   InterPro; IPR019913; Pyrimidine_utilisation_RutD.
DR   Pfam; PF12146; Hydrolase_4; 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..262
FT                   /note="Putative carbamate hydrolase RutD"
FT                   /id="PRO_0000402924"
SQ   SEQUENCE   262 AA;  28827 MW;  7346278FC6BC2DBC CRC64;
     MHFEVHGLDR PDAKTIILSS GLGGSGSYWA PQIEALATDF RIVTYDHRGT GRTGGDVPDT
     GGISAMADDV LEIAARLQLD RFDFMGHALG GLIGLDIALR RPELIGKLIL INAWSKADPH
     SGRCFDIRIE LLERSGVEAF VKAQPLFLYP AVWMSENAER MAADERHGVA HFQGKANVLK
     RIAALRAFDI DDRLSEIRTP TLVVGTRDDL LVPYTRSVRL AEGLSAAELA LSDFGAHAVN
     VVEPEEFNNK VLRFLRARSE VR