(data stored in ACNUC7421 zone)

SWISSPROT: RUTD_KLEP7

ID   RUTD_KLEP7              Reviewed;         266 AA.
AC   A6T799;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Putative aminoacrylate 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=KPN78578_10090; ORFNames=KPN_01035;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH
OS   78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May increase the rate of spontaneous hydrolysis of
CC       aminoacrylate to malonic semialdehyde. Required to remove a toxic
CC       intermediate produce in the pyrimidine nitrogen degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_00832}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(Z)-3-aminoacrylate + H(+) + H2O = 3-oxopropanoate +
CC         NH4(+); Xref=Rhea:RHEA:34947, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:33190,
CC         ChEBI:CHEBI:59894; Evidence={ECO:0000255|HAMAP-Rule:MF_00832};
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Hydrolase
CC       RutD family. {ECO:0000255|HAMAP-Rule:MF_00832}.
DR   EMBL; CP000647; ABR76470.1; -; Genomic_DNA.
DR   SMR; A6T799; -.
DR   ESTHER; klep7-a6t799; RutD.
DR   DNASU; 5339077; -.
DR   EnsemblBacteria; ABR76470; ABR76470; KPN_01035.
DR   KEGG; kpn:KPN_01035; -.
DR   eggNOG; ENOG41074FZ; Bacteria.
DR   eggNOG; COG0596; LUCA.
DR   HOGENOM; HOG000028072; -.
DR   KO; K09023; -.
DR   OMA; HAMSVTD; -.
DR   Proteomes; UP000000265; 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;
DR   PRODOM; A6T799.
DR   SWISS-2DPAGE; A6T799.
KW   Complete proteome; Hydrolase; Reference proteome.
FT   CHAIN         1    266       Putative aminoacrylate hydrolase RutD.
FT                                /FTId=PRO_0000402968.
FT   DOMAIN       14    239       AB hydrolase-1. {ECO:0000255}.
SQ   SEQUENCE   266 AA;  28248 MW;  C8B837107CF4D476 CRC64;
     MRLNIAPAPW PGAPVVVLSA GLGGGGGYWL AQRAALEEQY QLVSYDHNGT GENAGPLPAG
     YSLATMAGEL FSALQAAGIA RFALVGHALG ALIGLQLALD RPEAVSALAL VNGWLSLSPH
     TRRCFQVRER LLHAGGAQAW VEAQPLFLYP AEWMAARLPR LEAEDALAIS HFQGKENLLK
     RLQALKQADF SRRASAIACP TLIISAADDL LVPASCSRVL QTAIPGSQLV EMPWGGHACN
     VTDADTFNTI LRDGLSAMLP VARETR
//

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