RUTD_CAUVC
ID RUTD_CAUVC Reviewed; 269 AA.
AC Q9A4N3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=CC_2797;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK24761.1; -; Genomic_DNA.
DR PIR; E87595; E87595.
DR RefSeq; NP_421593.1; NC_002696.2.
DR RefSeq; WP_010920638.1; NC_002696.2.
DR AlphaFoldDB; Q9A4N3; -.
DR SMR; Q9A4N3; -.
DR STRING; 190650.CC_2797; -.
DR ESTHER; caucr-CC2797; RutD.
DR EnsemblBacteria; AAK24761; AAK24761; CC_2797.
DR KEGG; ccr:CC_2797; -.
DR PATRIC; fig|190650.5.peg.2799; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_020336_50_1_5; -.
DR OMA; HAMSVTD; -.
DR BioCyc; CAULO:CC2797-MON; -.
DR Proteomes; UP000001816; 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_0000402928"
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