ID   RUTD_PSEU2              Reviewed;         259 AA.
AC   Q4ZXS0;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=Psyr_0996;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY36052.1; -; Genomic_DNA.
DR   RefSeq; WP_011266759.1; NC_007005.1.
DR   RefSeq; YP_234090.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZXS0; -.
DR   SMR; Q4ZXS0; -.
DR   STRING; 205918.Psyr_0996; -.
DR   ESTHER; pseu2-q4zxs0; RutD.
DR   EnsemblBacteria; AAY36052; AAY36052; Psyr_0996.
DR   KEGG; psb:Psyr_0996; -.
DR   PATRIC; fig|205918.7.peg.1025; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_020336_50_1_6; -.
DR   OMA; HAMSVTD; -.
DR   Proteomes; UP000000426; 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; PF12697; Abhydrolase_6; 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..259
FT                   /note="Putative carbamate hydrolase RutD"
FT                   /id="PRO_0000402979"
SQ   SEQUENCE   259 AA;  28620 MW;  9B19902D2A8AC781 CRC64;
     MFHEFHACQH ADAPTLVLSS GLGGSGRYWA DDLTLLTRDY HVLVYDHAGT GRSPAVLPAD
     YSIRHMAIEL LALLDSLDIQ RCHFMGHALG GLVGLELALL RPELLHSQVL INAWSSPNPH
     SARCFSVRKK LLLNSGPEAY VQAQALFLYP ADWIAANGPR LADDEAHALA HFPDTDNLLR
     RIHALETFDV SAELSRIHTP TLLIANRDDM LVPWQQSRHL ANALPNATLV LLEYGGHASN
     ITDPLPFQRA LRAFLSTQP