ID   RUTD_ACIAD              Reviewed;         266 AA.
AC   Q6FFZ9;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=ACIAD0025;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG67008.1; -; Genomic_DNA.
DR   RefSeq; WP_004930959.1; NC_005966.1.
DR   AlphaFoldDB; Q6FFZ9; -.
DR   SMR; Q6FFZ9; -.
DR   STRING; 62977.ACIAD0025; -.
DR   ESTHER; aciad-q6ffz9; RutD.
DR   EnsemblBacteria; CAG67008; CAG67008; ACIAD0025.
DR   GeneID; 45232559; -.
DR   KEGG; aci:ACIAD0025; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_020336_50_1_6; -.
DR   OMA; HAMSVTD; -.
DR   OrthoDB; 1196738at2; -.
DR   BioCyc; ASP62977:ACIAD_RS00135-MON; -.
DR   Proteomes; UP000000430; 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   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR03611; RutD; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..266
FT                   /note="Putative carbamate hydrolase RutD"
FT                   /id="PRO_0000402923"
SQ   SEQUENCE   266 AA;  30161 MW;  477C1D38F1A10C2B CRC64;
     MNYQLFKHSD ENASYVVFSS GLGGHGSFWQ AQLDVFRQYF HVLIYDQEGC HASSELLADG
     YSFEHLALQV KQLLQQLNIV RFHFIGHALG GFIGIELAHR YASETCQLLS LTLINAWQQL
     DPHTLRCFTT RIALLQHAGT AAYLHAQALF LYPPLWISEH TALLEQQEAK MQSDFPPHAN
     VLKRLNALMQ YQVNTARIDT LKQLPVCLIA NQDDMLVPYV QSLNLWKKLP DAQLKLLPYG
     GHASTVTEAR QVNQLMLDFL KTSAPT