ID   RUTD_METEP              Reviewed;         260 AA.
AC   A9W3H8;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=Mext_1735;
OS   Methylorubrum extorquens (strain PA1) (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=419610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Marx C., Richardson P.;
RT   "Complete sequence of Methylobacterium extorquens PA1.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000908; ABY30134.1; -; Genomic_DNA.
DR   RefSeq; WP_012253314.1; NC_010172.1.
DR   AlphaFoldDB; A9W3H8; -.
DR   SMR; A9W3H8; -.
DR   STRING; 419610.Mext_1735; -.
DR   PRIDE; A9W3H8; -.
DR   EnsemblBacteria; ABY30134; ABY30134; Mext_1735.
DR   KEGG; mex:Mext_1735; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020336_50_1_5; -.
DR   OMA; HAMSVTD; -.
DR   BioCyc; MEXT419610:MEXT_RS08805-MON; -.
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.
FT   CHAIN           1..260
FT                   /note="Putative carbamate hydrolase RutD"
FT                   /id="PRO_0000402973"
FT   DOMAIN          17..117
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00832"
SQ   SEQUENCE   260 AA;  27631 MW;  E3BDD6E1D920359F CRC64;
     MAAPVHHEVH GPAGGRTVLL SPGLGGSAHY FAPQVPVLAE RFRVVTYDHR GTGRSPGPLE
     PGHDIAAMAR DVLDLLDLLD IGTADIVGHA LGGLIALQLA LTHPERVGRI VVINGWAVMD
     LATRRCFAAR KALLRHAGPE AFVRAQAIFL YPAPWLSENA ARVADDEAQA LAHFPGEETV
     LARIAALETF DATGALPRIP HETLLMAARD DVLVPYTASD ILAAGLPNAR LDLAPEGGHA
     HSVTRPEAFN RTLLDFLASP