ID   AC4CH_MORMI             Reviewed;         108 AA.
AC   Q9RA13;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 45.
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};
OS   Moritella marina (Vibrio marinus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=90736;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15381 / BCRC 15891 / CIP 102861 / NCIMB 1144 / MP-1;
RA   Tanaka M., Ueno A., Kawasaki K., Yumoto I., Ohgiya S., Hoshino T.,
RA   Ishizaki K., Okuyama H., Morita N.;
RT   "Isolation of clustered genes that are notably homologous to the
RT   eicosapentaenoic acid biosynthesis gene cluster from the docosahexaenoic
RT   acid-producing bacterium Vibrio marinus strain MP-1.";
RL   Biotechnol. Lett. 21:939-945(1999).
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; AB025342; BAA89390.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RA13; -.
DR   SMR; Q9RA13; -.
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..108
FT                   /note="N(4)-acetylcytidine amidohydrolase"
FT                   /id="PRO_0000214609"
FT   DOMAIN          5..102
FT                   /note="ASCH"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        20
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00684"
FT   ACT_SITE        23
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00684"
FT   ACT_SITE        73
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00684"
SQ   SEQUENCE   108 AA;  12632 MW;  5C40FC8E6F5E9781 CRC64;
     MYSCITFFQR LERSILSGNK TATIRDKSDS HYLVGQMLDA CTHEDNRKMC QIEILSIEYV
     TFSELNRAHA NAEGLPFLFM LKWIVRKIYP TSNDLFFISF RVVTIDIL