ID A0A0A3ARB0_9PAST Unreviewed; 105 AA.
AC A0A0A3ARB0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=N(4)-acetylcytidine amidohydrolase {ECO:0000256|HAMAP-Rule:MF_00684};
DE Short=ac4C amidohydrolase {ECO:0000256|HAMAP-Rule:MF_00684};
DE EC=3.5.1.135 {ECO:0000256|HAMAP-Rule:MF_00684};
GN ORFNames=OA57_07230 {ECO:0000313|EMBL:KGQ70292.1};
OS Chelonobacter oris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Chelonobacter.
OX NCBI_TaxID=505317 {ECO:0000313|EMBL:KGQ70292.1, ECO:0000313|Proteomes:UP000030380};
RN [1] {ECO:0000313|EMBL:KGQ70292.1, ECO:0000313|Proteomes:UP000030380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1662 {ECO:0000313|EMBL:KGQ70292.1,
RC ECO:0000313|Proteomes:UP000030380};
RA Kudirkiene E., Hansen M.J., Bojesen A.M.;
RT "Draft genome sequence of Chelonobacter oris 1662T, associated with
RT respiratory disease in Hermann's Tortoises.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of N(4)-acetylcytidine (ac4C).
CC {ECO:0000256|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:0000256|HAMAP-
CC 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:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_00684};
CC -!- SIMILARITY: Belongs to the N(4)-acetylcytidine amidohydrolase family.
CC {ECO:0000256|HAMAP-Rule:MF_00684}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGQ70292.1}.
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DR EMBL; JSUM01000011; KGQ70292.1; -; Genomic_DNA.
DR RefSeq; WP_034615609.1; NZ_JSUM01000011.1.
DR AlphaFoldDB; A0A0A3ARB0; -.
DR STRING; 505317.OA57_07230; -.
DR OrthoDB; 8590202at2; -.
DR Proteomes; UP000030380; Unassembled WGS sequence.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:UniProtKB-UniRule.
DR CDD; cd06552; ASCH_yqfb_like; 1.
DR Gene3D; 2.30.130.30; Hypothetical protein; 1.
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; UCP029143 FAMILY PROTEIN; 1.
DR PANTHER; PTHR38088:SF2; UCP029143 FAMILY PROTEIN; 1.
DR Pfam; PF04266; ASCH; 1.
DR PIRSF; PIRSF029143; UCP029143; 1.
DR SMART; SM01022; ASCH; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00684};
KW Reference proteome {ECO:0000313|Proteomes:UP000030380}.
FT DOMAIN 7..105
FT /note="ASCH"
FT /evidence="ECO:0000259|SMART:SM01022"
FT ACT_SITE 22
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00684"
FT ACT_SITE 25
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00684"
FT ACT_SITE 75
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00684"
SQ SEQUENCE 105 AA; 12372 MW; D7D341EF1128FC1A CRC64;
MIPPTQITFF QRFEADILNG SKTITIRDQA ESHYLPDSVV DVLTYEMQRW FAKIRILSVT
PITFNQLNQR HASQENMLLS ELKEVIREIY PNETALWVLE FELIS
//
