RUTD_ECO24
ID RUTD_ECO24 Reviewed; 266 AA.
AC A7ZKB4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 66.
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};
GN OrderedLocusNames=EcE24377A_1127;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV16624.1; -; Genomic_DNA.
DR RefSeq; WP_012138029.1; NC_009801.1.
DR AlphaFoldDB; A7ZKB4; -.
DR SMR; A7ZKB4; -.
DR ESTHER; ecoli-rutD; RutD.
DR EnsemblBacteria; ABV16624; ABV16624; EcE24377A_1127.
DR KEGG; ecw:EcE24377A_1127; -.
DR HOGENOM; CLU_020336_50_1_6; -.
DR OMA; HAMSVTD; -.
DR Proteomes; UP000001122; 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.
FT CHAIN 1..266
FT /note="Putative carbamate hydrolase RutD"
FT /id="PRO_0000402950"
SQ SEQUENCE 266 AA; 28992 MW; A1C9B5036E81A947 CRC64;
MKLSLSPPPY ADAPVVVLIS GLGGSGSYWL PQLAVLEQEY QVVCYDQRGT GNNPDTLAED
YSITQMAAEL HQALVAAGIE RYAVVGHALG ALVGMQLALD YPASVTVLIS VNGWLRINAH
TRRCFQVRER LLYSGGAQAW VEAQPLFLYP ADWMAARAPR LEAEDALALA HFQGKNNLLR
RLNALKRADF SHHADRIRCP VQIICASDDL LVPSACSSEL HAALPDSQKM VMRYGGHACN
VTDPETFNAL LLNGLASLLH HREAAL