RUTD_ECOUT
ID RUTD_ECOUT Reviewed; 275 AA.
AC Q1RDK8;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=UTI89_C1072;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE06556.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1RDK8; -.
DR SMR; Q1RDK8; -.
DR ESTHER; ecoli-rutD; RutD.
DR EnsemblBacteria; ABE06556; ABE06556; UTI89_C1072.
DR KEGG; eci:UTI89_C1072; -.
DR HOGENOM; CLU_020336_50_1_6; -.
DR OMA; HAMSVTD; -.
DR Proteomes; UP000001952; 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..275
FT /note="Putative carbamate hydrolase RutD"
FT /id="PRO_0000402946"
SQ SEQUENCE 275 AA; 29821 MW; 23F5B04722956F7E CRC64;
MRISPSEAAM KLSLSPPPYA DAPVVVLISG LGGSGSYWLP QLAVLVQEYQ VVCYDQRGTG
NNPDTLAEDY SIAQMAAELH QALVAAGIER YAVVGHALGA LVGMQLALDY PASVTVLVSV
NGWLRINAHT RRCFQVREQL LHSGGAQAWV EAQPLFLYPA DWMAARAPRL EAEDALALAH
FQGKNNLLRR LNALKRADFS HHADRIRCPV QIICASDDLL VPTACSSELH AALPDSQKMV
MRYGGHACNV TDPETFNALL LNGLASLLHH REAAL