ID D2U8N4_XANAP Unreviewed; 365 AA.
AC D2U8N4;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=N-acetyl-L-citrulline deacetylase {ECO:0000256|HAMAP-Rule:MF_02236};
DE Short=ACDase {ECO:0000256|HAMAP-Rule:MF_02236};
DE Short=Acetylcitrulline deacetylase {ECO:0000256|HAMAP-Rule:MF_02236};
DE EC=3.5.1.- {ECO:0000256|HAMAP-Rule:MF_02236};
GN Name=argE {ECO:0000313|EMBL:CBA16382.1};
GN Synonyms=argE' {ECO:0000256|HAMAP-Rule:MF_02236};
GN OrderedLocusNames=XALc_1893 {ECO:0000313|EMBL:CBA16382.1};
OS Xanthomonas albilineans (strain GPE PC73 / CFBP 7063).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA16382.1, ECO:0000313|Proteomes:UP000001890};
RN [1] {ECO:0000313|EMBL:CBA16382.1, ECO:0000313|Proteomes:UP000001890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890};
RX PubMed=20017926; DOI=10.1186/1471-2164-10-616;
RA Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., Cociancich S.,
RA Couloux A., Darrasse A., Gouzy J., Jacques M.A., Lauber E., Manceau C.,
RA Mangenot S., Poussier S., Segurens B., Szurek B., Verdier V., Arlat M.,
RA Rott P.;
RT "The complete genome sequence of Xanthomonas albilineans provides new
RT insights into the reductive genome evolution of the xylem-limited
RT Xanthomonadaceae.";
RL BMC Genomics 10:616-616(2009).
CC -!- FUNCTION: Catalyzes the deacetylation of N-acetyl-L-citrulline to
CC produce L-citrulline. This is a step in an alternative arginine
CC biosynthesis pathway. {ECO:0000256|HAMAP-Rule:MF_02236}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-acetyl-L-citrulline = acetate + L-citrulline;
CC Xref=Rhea:RHEA:61092, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57743, ChEBI:CHEBI:58765; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02236};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02236};
CC Note=Binds 1 Co(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_02236};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02236}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. N-acetylcitrulline
CC deacetylase subfamily. {ECO:0000256|HAMAP-Rule:MF_02236}.
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DR EMBL; FP565176; CBA16382.1; -; Genomic_DNA.
DR RefSeq; WP_012916381.1; NC_013722.1.
DR AlphaFoldDB; D2U8N4; -.
DR STRING; 380358.XALC_1893; -.
DR GeneID; 57877196; -.
DR KEGG; xal:XALC_1893; -.
DR PATRIC; fig|29447.3.peg.1846; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 3665926at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001890; Chromosome.
DR GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR GO; GO:0043909; F:N-acetylcitrulline deacetylase activity; IEA:RHEA.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_02236; ACDase; 1.
DR InterPro; IPR043697; ACDase_ArgE'-like.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF1; ACETYLORNITHINE DEACETYLASE; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02236};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_02236}; Cobalt {ECO:0000256|HAMAP-Rule:MF_02236};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02236};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_02236}; Reference proteome {ECO:0000313|Proteomes:UP000001890}.
FT DOMAIN 163..269
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 129
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02236"
FT BINDING 71
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02236"
FT BINDING 102
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02236"
FT BINDING 154
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02236"
SQ SEQUENCE 365 AA; 38839 MW; B5B1177782092FF8 CRC64;
MTDLLTSTLD HLQALVAFDT RNPPRAITTA GIFDYLRAKL PGFRVEVIDH GAGAVSLYAV
RGTPKYLFNV HLDTVPDSPH WSADPHVMRR TEDRVIGLGV CDIKGAAAAL IAAANAGDGD
AAFLFSSDEE ANDPRCIAAF LARGIAYEAV LVAEPTMSDA VLAHRGISSV LMRFAGRAGH
ASGKQDPSAS ALHQAIRWGG RALDHVESLA HARFGGLTGL RFNIGRVEGG IKANMIAPAT
EVRFGFRPLP SMDVDALLGS FAGFADPAAA HFEETFRGPS LPSGDIARAE ERRLAARDVA
DALELPIGNA VDFWTEASLF SAGGYTALVY GPGDIAQAHT ADEFVTLEQL QRYATSVHRI
LNGVR
//
