AC4CH_VIBPA
ID AC4CH_VIBPA Reviewed; 107 AA.
AC Q87GA3;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=VPA1414;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000032; BAC62757.1; -; Genomic_DNA.
DR RefSeq; NP_800924.1; NC_004605.1.
DR RefSeq; WP_005478088.1; NC_004605.1.
DR AlphaFoldDB; Q87GA3; -.
DR SMR; Q87GA3; -.
DR STRING; 223926.28809782; -.
DR EnsemblBacteria; BAC62757; BAC62757; BAC62757.
DR GeneID; 1192110; -.
DR KEGG; vpa:VPA1414; -.
DR PATRIC; fig|223926.6.peg.4341; -.
DR eggNOG; COG3097; Bacteria.
DR HOGENOM; CLU_152586_0_0_6; -.
DR OMA; HARQENM; -.
DR Proteomes; UP000002493; Chromosome 2.
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; Reference proteome.
FT CHAIN 1..107
FT /note="N(4)-acetylcytidine amidohydrolase"
FT /id="PRO_0000214610"
FT DOMAIN 9..105
FT /note="ASCH"
FT /evidence="ECO:0000255"
FT ACT_SITE 23
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00684"
FT ACT_SITE 26
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00684"
FT ACT_SITE 76
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00684"
SQ SEQUENCE 107 AA; 12570 MW; 40F604651F65E1CC CRC64;
MSSHPTKITF FEFLTPLITS GQKTITIRDE SESHYVPNTE VEVFTLETDR KVCDIKILSV
EPLNFDEINE FHAEQEAIEL PKLKQLIREI YPNIDKLFVI EYELIKK
