ID   RUTD_PANAM              Reviewed;         275 AA.
AC   D4GEU7;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=PANA_4036;
OS   Pantoea ananatis (strain LMG 20103).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=706191;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20103;
RX   PubMed=20348253; DOI=10.1128/jb.00060-10;
RA   De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA   Coutinho T.A.;
RT   "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT   Eucalyptus blight and dieback.";
RL   J. Bacteriol. 192:2936-2937(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; CP001875; ADD79203.1; -; Genomic_DNA.
DR   RefSeq; WP_013027869.1; NC_013956.2.
DR   AlphaFoldDB; D4GEU7; -.
DR   SMR; D4GEU7; -.
DR   STRING; 706191.PANA_4036; -.
DR   EnsemblBacteria; ADD79203; ADD79203; PANA_4036.
DR   KEGG; pam:PANA_4036; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020336_50_1_6; -.
DR   OMA; HAMSVTD; -.
DR   OrthoDB; 1196738at2; -.
DR   BioCyc; PANA706191:PANA_RS20510-MON; -.
DR   Proteomes; UP000001702; 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..275
FT                   /note="Putative carbamate hydrolase RutD"
FT                   /id="PRO_0000402976"
FT   DOMAIN          15..116
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00832"
SQ   SEQUENCE   275 AA;  30097 MW;  1DAEC4539368EB73 CRC64;
     MYYKVLGQQN ADAETVVLSS GLGGSGGFWQ PQLAMLSAHF RVVVYDQYGT GASQGSVPAG
     YRMEDMADEL AGLLNALNIS RCHLVGHALG GIMGLHLALR YPALLQSLVV INGWTVLNSQ
     TRRCFDVRRN LLLNSGVDAY VQAQPLFLYP GDWLSEHEAF LQEERQHQVA NFQGMENLLH
     RLQALMDSDL TTSLKGVIAP TLALSAKDDL LVPWSCSADL ASRLPHGEHL QMGYGGHAMS
     VTDPDTFNPI LLDWLQRQAS HPSGTPSDFI PVEMP