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AC4CH_ECOSM
ID   AC4CH_ECOSM             Reviewed;         103 AA.
AC   B1LDA1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=EcSMS35_3033;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
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; CP000970; ACB18959.1; -; Genomic_DNA.
DR   RefSeq; WP_001182958.1; NC_010498.1.
DR   AlphaFoldDB; B1LDA1; -.
DR   BMRB; B1LDA1; -.
DR   SMR; B1LDA1; -.
DR   EnsemblBacteria; ACB18959; ACB18959; EcSMS35_3033.
DR   KEGG; ecm:EcSMS35_3033; -.
DR   HOGENOM; CLU_152586_0_0_6; -.
DR   OMA; HARQENM; -.
DR   Proteomes; UP000007011; 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_1000131789"
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;  11841 MW;  89B1DC8387D6F2CC CRC64;
     MQPNDITFFQ RFQDDILAGR KTITIRDESE SHFKTGDVLR VGRFEDDGYF CTIEVTATST
     VTLDTLTEKH AGQENMTLPE LKKVIADIYP GQIQFYVIEF KCL
 
 
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