AC4CH_SALPK
ID AC4CH_SALPK Reviewed; 103 AA.
AC B5BFL5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 56.
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=SSPA2720;
OS Salmonella paratyphi A (strain AKU_12601).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=554290;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AKU_12601;
RX PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA Mungall K., Dougan G., Parkhill J.;
RT "Pseudogene accumulation in the evolutionary histories of Salmonella
RT enterica serovars Paratyphi A and Typhi.";
RL BMC Genomics 10:36-36(2009).
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; FM200053; CAR60961.1; -; Genomic_DNA.
DR RefSeq; WP_001182976.1; NC_011147.1.
DR AlphaFoldDB; B5BFL5; -.
DR SMR; B5BFL5; -.
DR KEGG; sek:SSPA2720; -.
DR HOGENOM; CLU_152586_0_0_6; -.
DR OMA; HARQENM; -.
DR Proteomes; UP000001869; 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_1000131798"
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
