AC4CH_SHIB3
ID AC4CH_SHIB3 Reviewed; 103 AA.
AC B2U0R7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=SbBS512_E3321;
OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=344609;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 3083-94 / BS512;
RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA Jiang L., Ravel J., Sebastian Y.;
RT "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001063; ACD09096.1; -; Genomic_DNA.
DR RefSeq; WP_001182969.1; NC_010658.1.
DR AlphaFoldDB; B2U0R7; -.
DR SMR; B2U0R7; -.
DR STRING; 344609.SbBS512_E3321; -.
DR EnsemblBacteria; ACD09096; ACD09096; SbBS512_E3321.
DR KEGG; sbc:SbBS512_E3321; -.
DR HOGENOM; CLU_152586_0_0_6; -.
DR OMA; HARQENM; -.
DR Proteomes; UP000001030; 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_1000131800"
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; 11908 MW; 5AD4F3AB96D545F4 CRC64;
MQPNDITFFQ RFQDDIMAGR KTITIRDESE SHFKTGDVLR VGRFEDDGYF CTIEVTATST
VTLDTLTEKH AEQENMTLTE LIKVIADIYP GQTQFYVIEF KCL
