ID   AC4CH_ECOL6             Reviewed;         103 AA.
AC   Q8FE69;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=N(4)-acetylcytidine amidohydrolase {ECO:0000255|HAMAP-Rule:MF_00684};
DE            Short=ac4C amidohydrolase {ECO:0000255|HAMAP-Rule:MF_00684};
DE            EC=3.5.1.135 {ECO:0000255|HAMAP-Rule:MF_00684};
GN   Name=yqfB; OrderedLocusNames=c3481;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the hydrolysis of N(4)-acetylcytidine (ac4C).
CC       {ECO:0000255|HAMAP-Rule:MF_00684}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(4)-acetylcytidine = acetate + cytidine + H(+);
CC         Xref=Rhea:RHEA:62932, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17562, ChEBI:CHEBI:30089, ChEBI:CHEBI:70989;
CC         EC=3.5.1.135; Evidence={ECO:0000255|HAMAP-Rule:MF_00684};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(4)-acetyl-2'-deoxycytidine = 2'-deoxycytidine +
CC         acetate + H(+); Xref=Rhea:RHEA:62936, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:146133; EC=3.5.1.135; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00684};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(4)-acetylcytosine = acetate + cytosine + H(+);
CC         Xref=Rhea:RHEA:62940, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16040, ChEBI:CHEBI:30089, ChEBI:CHEBI:146134;
CC         EC=3.5.1.135; Evidence={ECO:0000255|HAMAP-Rule:MF_00684};
CC   -!- SIMILARITY: Belongs to the N(4)-acetylcytidine amidohydrolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00684}.
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DR   EMBL; AE014075; AAN81929.1; -; Genomic_DNA.
DR   RefSeq; WP_001182956.1; NC_004431.1.
DR   AlphaFoldDB; Q8FE69; -.
DR   SMR; Q8FE69; -.
DR   STRING; 199310.c3481; -.
DR   EnsemblBacteria; AAN81929; AAN81929; c3481.
DR   KEGG; ecc:c3481; -.
DR   eggNOG; COG3097; Bacteria.
DR   HOGENOM; CLU_152586_0_0_6; -.
DR   OMA; HARQENM; -.
DR   BioCyc; ECOL199310:C3481-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:UniProtKB-UniRule.
DR   GO; GO:0106251; F:N4-acetylcytidine amidohydrolase activity; IEA:RHEA.
DR   HAMAP; MF_00684; ac4C_amidohydr; 1.
DR   InterPro; IPR008314; AC4CH.
DR   InterPro; IPR007374; ASCH_domain.
DR   InterPro; IPR015947; PUA-like_sf.
DR   PANTHER; PTHR38088; PTHR38088; 1.
DR   Pfam; PF04266; ASCH; 1.
DR   PIRSF; PIRSF029143; UCP029143; 1.
DR   SMART; SM01022; ASCH; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..103
FT                   /note="N(4)-acetylcytidine amidohydrolase"
FT                   /id="PRO_0000214602"
FT   DOMAIN          6..101
FT                   /note="ASCH"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        21
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00684"
FT   ACT_SITE        24
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00684"
FT   ACT_SITE        74
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00684"
SQ   SEQUENCE   103 AA;  11963 MW;  BBC4E2AA8419F2CE CRC64;
     MQPNDITFFQ RFQDDILAGR KTITIRDESE SHFKTGDVLR VGRFEDDGYF CTIEVTATST
     VTLDTLTEKH AEQENMTLTE LKKVIADIYP DQTQFYVIEF KCL