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AC4CH_VIBCM
ID   AC4CH_VIBCM             Reviewed;         105 AA.
AC   C3LMQ4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 51.
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   OrderedLocusNames=VCM66_1516;
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(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; CP001233; ACP05830.1; -; Genomic_DNA.
DR   RefSeq; WP_000028411.1; NC_012578.1.
DR   AlphaFoldDB; C3LMQ4; -.
DR   SMR; C3LMQ4; -.
DR   EnsemblBacteria; ACP05830; ACP05830; VCM66_1516.
DR   GeneID; 57740231; -.
DR   KEGG; vcm:VCM66_1516; -.
DR   HOGENOM; CLU_152586_0_0_6; -.
DR   OMA; HARQENM; -.
DR   Proteomes; UP000001217; Chromosome I.
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..105
FT                   /note="N(4)-acetylcytidine amidohydrolase"
FT                   /id="PRO_1000147753"
FT   DOMAIN          8..93
FT                   /note="ASCH"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        22
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00684"
FT   ACT_SITE        25
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00684"
FT   ACT_SITE        75
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00684"
SQ   SEQUENCE   105 AA;  12119 MW;  3A3DBF8AAD90756B CRC64;
     MSISTQITFF EFLTPLVASG QKTITIRDKS ESHYVPGTRV EVFTLETQRK VCEIDILAVE
     PLKFDEINEF HAEQEAIELP KLKALIQEIY PNIDELYVIT YQLAK
 
 
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