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RUTD_SHIFL
ID   RUTD_SHIFL              Reviewed;         266 AA.
AC   Q83LK8; Q7UCZ9;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 4.
DT   25-MAY-2022, entry version 113.
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=SF1012, S1082;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN42638.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16523.1; -; Genomic_DNA.
DR   RefSeq; NP_706931.2; NC_004337.2.
DR   RefSeq; WP_000777662.1; NZ_WPGW01000134.1.
DR   AlphaFoldDB; Q83LK8; -.
DR   SMR; Q83LK8; -.
DR   STRING; 198214.SF1012; -.
DR   ESTHER; shifl-YCDJ; RutD.
DR   EnsemblBacteria; AAN42638; AAN42638; SF1012.
DR   EnsemblBacteria; AAP16523; AAP16523; S1082.
DR   GeneID; 1023981; -.
DR   KEGG; sfl:SF1012; -.
DR   KEGG; sft:NCTC1_01051; -.
DR   KEGG; sfx:S1082; -.
DR   PATRIC; fig|198214.7.peg.1176; -.
DR   HOGENOM; CLU_020336_50_1_6; -.
DR   OMA; HAMSVTD; -.
DR   OrthoDB; 1196738at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Reference proteome.
FT   CHAIN           1..266
FT                   /note="Putative carbamate hydrolase RutD"
FT                   /id="PRO_0000402982"
FT   DOMAIN          14..115
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00832"
SQ   SEQUENCE   266 AA;  28925 MW;  F538FAD4E479DE77 CRC64;
     MKLSLSSPPY ADAPVVVLIS GLGGSGSYWL PQLAVLEQEY QVVCYDQRGT GNNPDTLAED
     YSIAQMAAEL HQALVAAGIE RYAVVGHALG ALVGMQLALD YPASVTMLVS VNGWLRINAH
     TRRCFQVRER LLYSGGAQAW VEAQPLFLYP ADWMAARAPR LEAEDALALA HFQGKNNLLR
     RLNALKRADF SHHADRIRCP VQIICASDDL LVPTACSSEL HAALPDSQKM VMPYGGHACN
     VTDPETFNAL LLNGLASLLH HREAAL
 
 
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