ID   AC4CH_SALPA             Reviewed;         103 AA.
AC   Q5PJF2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=SPA2918;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV78759.1; -; Genomic_DNA.
DR   RefSeq; WP_001182976.1; NC_006511.1.
DR   AlphaFoldDB; Q5PJF2; -.
DR   SMR; Q5PJF2; -.
DR   EnsemblBacteria; AAV78759; AAV78759; SPA2918.
DR   KEGG; spt:SPA2918; -.
DR   HOGENOM; CLU_152586_0_0_6; -.
DR   OMA; HARQENM; -.
DR   Proteomes; UP000008185; 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_1000044952"
FT   DOMAIN          6..94
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;  11899 MW;  417DCFD551D1317B CRC64;
     MQPNDITFFQ RFQNDILAGR KTITIRDASE SHFKAGDVLR VGRFEDDGYF CTIEVTGTST
     VTLDTLNEKH AQQENMSLDE LKRVIAEIYP NQTQFYVIDF KCL