RUTD_KLEP3
ID RUTD_KLEP3 Reviewed; 266 AA.
AC B5XXN3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 58.
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=KPK_3523;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(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; CP000964; ACI11680.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XXN3; -.
DR SMR; B5XXN3; -.
DR EnsemblBacteria; ACI11680; ACI11680; KPK_3523.
DR KEGG; kpe:KPK_3523; -.
DR HOGENOM; CLU_020336_50_1_6; -.
DR OMA; HAMSVTD; -.
DR Proteomes; UP000001734; 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_0000402967"
FT DOMAIN 14..238
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00832"
SQ SEQUENCE 266 AA; 28287 MW; 3F2DAE81374695AB CRC64;
MRLNIAPAPW PGAPVVVLSA GLGGGGGYWL AQRAALEAQY QLVSYDHNGT GENAGPLPAD
YSMATMAQEL LSALQAAGIT RFALVGHALG ALIGLQLALD RPEAVSALVL VNGWLTLSPH
TRRCFLVRER LLHAGGAQAW VEAQPLFLYP AEWMAARLPR LEAEDALAIS HFQGKENLLK
RLQALKQADF SRRAAAIACP TLIVSAADDL LVPASCSRVL QAAIPGSQRV EMPWGGHACN
VTDADTFNTI LCDGLAAMLP VAREIR