RUTD_ECOCB
ID RUTD_ECOCB Reviewed; 266 AA.
AC D3QPK2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 25-MAY-2022, entry version 46.
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=G2583_1242;
OS Escherichia coli O55:H7 (strain CB9615 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=701177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB9615 / EPEC;
RX PubMed=20090843; DOI=10.1371/journal.pone.0008700;
RA Zhou Z., Li X., Liu B., Beutin L., Xu J., Ren Y., Feng L., Lan R.,
RA Reeves P.R., Wang L.;
RT "Derivation of Escherichia coli O157:H7 from its O55:H7 precursor.";
RL PLoS ONE 5:E8700-E8700(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; CP001846; ADD55840.1; -; Genomic_DNA.
DR RefSeq; WP_001301780.1; NC_013941.1.
DR AlphaFoldDB; D3QPK2; -.
DR SMR; D3QPK2; -.
DR ESTHER; ecoli-rutD; RutD.
DR EnsemblBacteria; ADD55840; ADD55840; G2583_1242.
DR KEGG; eok:G2583_1242; -.
DR HOGENOM; CLU_020336_50_1_6; -.
DR OMA; HAMSVTD; -.
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; IPR022742; Hydrolase_4.
DR InterPro; IPR019913; Pyrimidine_utilisation_RutD.
DR Pfam; PF12146; Hydrolase_4; 1.
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_0000402960"
SQ SEQUENCE 266 AA; 28949 MW; 7F7980BAC6F33A32 CRC64;
MKLSLSPPPY ADAPVVVLIS GLGGSGSYWL PQLAVLEQEY QVVCYDQRGT GNNPDTLAED
YSITQMAAEL HQALVAAGIE HYAVVGHALG ALVGMQLALD HPASVTVLVC VNGWLRINAH
TRRCFQVRER LLYSGGAQAW VEAQPLFLYP ADWMAARAPR LEAEDALALA HFQGKNNLLR
RLNALKRADF SHHADRIRCP VQIICASDDL LVPSACSSEL HAALPDSQKM VMRYGGHACN
VTDPETFNAL LLNGLASLLH HREAAL