AC4CH_VIBC3
ID AC4CH_VIBC3 Reviewed; 114 AA.
AC A5F7V7; C3M0Y1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 65.
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=VC0395_A1180, VC395_1692;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
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; CP000627; ABQ21015.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP09697.1; -; Genomic_DNA.
DR RefSeq; WP_000115900.1; NZ_JAACZH010000009.1.
DR AlphaFoldDB; A5F7V7; -.
DR SMR; A5F7V7; -.
DR STRING; 345073.VC395_1692; -.
DR EnsemblBacteria; ABQ21015; ABQ21015; VC0395_A1180.
DR KEGG; vco:VC0395_A1180; -.
DR KEGG; vcr:VC395_1692; -.
DR PATRIC; fig|345073.21.peg.1638; -.
DR eggNOG; COG3097; Bacteria.
DR HOGENOM; CLU_152586_0_0_6; -.
DR OMA; HARQENM; -.
DR Proteomes; UP000000249; 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.
FT CHAIN 1..114
FT /note="N(4)-acetylcytidine amidohydrolase"
FT /id="PRO_1000072734"
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 114 AA; 13075 MW; B164B7476DE114DA CRC64;
MSVPTQITFF EFLTPLVASG QKTITIRDKS ESHYVPGTRV EVFTLETQRK VCEIDILAVE
PLKFDEINEF HAEQEAIELP KLKALIQEIY PNIDELYVIT YQLAKSSSAR IMVK
