AC4CH_ECO55
ID AC4CH_ECO55 Reviewed; 103 AA.
AC B7LF85;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, 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=EC55989_3187;
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(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; CU928145; CAU99151.1; -; Genomic_DNA.
DR RefSeq; WP_001182954.1; NC_011748.1.
DR AlphaFoldDB; B7LF85; -.
DR SMR; B7LF85; -.
DR EnsemblBacteria; CAU99151; CAU99151; EC55989_3187.
DR GeneID; 58460562; -.
DR KEGG; eck:EC55989_3187; -.
DR HOGENOM; CLU_152586_0_0_6; -.
DR OMA; HARQENM; -.
DR Proteomes; UP000000746; 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_1000147749"
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; 11890 MW; BBC4E2AA87D5442E CRC64;
MQPNDITFFQ RFQDDILAGR KTITIRDESE SHFKTGDVLR VGRFEDDGYF CTIEVTATST
VTLDTLTEKH AEQENMTLTE LIKVIADIYP GQTQFYVIEF KCL