ID A0A0A0F1X6_9GAMM Unreviewed; 369 AA.
AC A0A0A0F1X6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:0000256|HAMAP-Rule:MF_02236};
GN ORFNames=N799_07200 {ECO:0000313|EMBL:KGM55362.1};
OS Lysobacter arseniciresistens ZS79.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=913325 {ECO:0000313|EMBL:KGM55362.1, ECO:0000313|Proteomes:UP000029989};
RN [1] {ECO:0000313|EMBL:KGM55362.1, ECO:0000313|Proteomes:UP000029989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS79 {ECO:0000313|EMBL:KGM55362.1,
RC ECO:0000313|Proteomes:UP000029989};
RX PubMed=26516404; DOI=10.1186/s40793-015-0070-5;
RA Liu L., Zhang S., Luo M., Wang G.;
RT "Genomic information of the arsenic-resistant bacterium Lysobacter
RT arseniciresistens type strain ZS79(T) and comparison of Lysobacter draft
RT genomes.";
RL Stand. Genomic Sci. 10:88-88(2015).
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}.
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:KGM55362.1}.
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DR EMBL; AVPT01000019; KGM55362.1; -; Genomic_DNA.
DR RefSeq; WP_036211725.1; NZ_AVPT01000019.1.
DR AlphaFoldDB; A0A0A0F1X6; -.
DR STRING; 913325.N799_07200; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 3665926at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000029989; Unassembled WGS sequence.
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:UP000029989}.
FT DOMAIN 165..270
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 126
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02236"
FT BINDING 68
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02236"
FT BINDING 99
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02236"
FT BINDING 156
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02236"
SQ SEQUENCE 369 AA; 39367 MW; E9C36DF95B07E9A6 CRC64;
MLPDILRHLE ALVAFDTRNP PRRIGTGGMF DYLRAQLPGF RIDVTDHGDG AVSMLAVRGR
PRRLFNVHLD TVPSSPAWSG DPHVLRVTGD RAIGLGACDI KGAAAGLLAA ATRTSGDAAF
LFSTDEEAND ARCIATFLKR NAPGGDLGFS EAIIAEPTRC EAVLAHRGIS SVLMHFRGSA
GHASGANAME ASALHQAMRW GDRALDLVEA EAPQRFGGLT GLRFNIGRVE GGIKANMIAP
SAELRFGFRP LPSMSIDALH ARFGTLVEAG AVARYEETFR GPPLPAGDVA DAEERRLQAR
DLAEALDLPI GNAVDFWTEA SLFSDAGMTA LVYGPGDIAQ AHTADEWVAL EQLQRYGESV
TRILDGVSM
//
