ID RUTD_SHIF2 Reviewed; 266 AA. AC D2AC40; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 09-FEB-2010, sequence version 1. DT 25-MAY-2022, entry version 49. 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=SFxv_1098; OS Shigella flexneri serotype X (strain 2002017). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=591020; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2002017; RX PubMed=19955273; DOI=10.1128/jcm.00614-09; RA Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z., RA Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X., RA Bai X., Wang Y., Wang P., Xu Q., Xu J.; RT "Emergence of a new multidrug-resistant serotype X variant in an epidemic RT clone of Shigella flexneri."; RL J. Clin. Microbiol. 48:419-426(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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001383; ADA73358.1; -; Genomic_DNA. DR RefSeq; WP_000777662.1; NC_017328.1. DR AlphaFoldDB; D2AC40; -. DR SMR; D2AC40; -. DR ESTHER; shifl-YCDJ; RutD. DR EnsemblBacteria; ADA73358; ADA73358; SFxv_1098. DR KEGG; sfe:SFxv_1098; -. DR PATRIC; fig|591020.3.peg.1172; -. DR HOGENOM; CLU_020336_50_1_6; -. DR OMA; HAMSVTD; -. DR Proteomes; UP000001884; 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. FT CHAIN 1..266 FT /note="Putative carbamate hydrolase RutD" FT /id="PRO_0000402984" FT DOMAIN 14..115 FT /note="AB hydrolase-1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00832" SQ SEQUENCE 266 AA; 28925 MW; F538FAD4E479DE77 CRC64; MKLSLSSPPY ADAPVVVLIS GLGGSGSYWL PQLAVLEQEY QVVCYDQRGT GNNPDTLAED YSIAQMAAEL HQALVAAGIE RYAVVGHALG ALVGMQLALD YPASVTMLVS VNGWLRINAH TRRCFQVRER LLYSGGAQAW VEAQPLFLYP ADWMAARAPR LEAEDALALA HFQGKNNLLR RLNALKRADF SHHADRIRCP VQIICASDDL LVPTACSSEL HAALPDSQKM VMPYGGHACN VTDPETFNAL LLNGLASLLH HREAAL //