ID B2FME0_STRMK Unreviewed; 362 AA.
AC B2FME0;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 OrderedLocusNames=Smlt3300 {ECO:0000313|EMBL:CAQ46735.1};
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ46735.1, ECO:0000313|Proteomes:UP000008840};
RN [1] {ECO:0000313|EMBL:CAQ46735.1, ECO:0000313|Proteomes:UP000008840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a {ECO:0000313|EMBL:CAQ46735.1,
RC ECO:0000313|Proteomes:UP000008840};
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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; AM743169; CAQ46735.1; -; Genomic_DNA.
DR RefSeq; WP_012480829.1; NC_010943.1.
DR AlphaFoldDB; B2FME0; -.
DR EnsemblBacteria; CAQ46735; CAQ46735; Smlt3300.
DR KEGG; sml:Smlt3300; -.
DR PATRIC; fig|522373.3.peg.3094; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_0_6; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000008840; Chromosome.
DR GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule.
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:UP000008840}.
FT DOMAIN 160..266
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 151
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02236"
SQ SEQUENCE 362 AA; 38481 MW; 197D500008E2EE0A CRC64;
MLEQTLDHLQ ALVSFDTRNP PRAITTGGIF DYLRDNLPGF NLEVIDHGAG AVSLYAVRGT
PKYLFNVHLD TVPDSPHWSA DPHVMRRLDD RVVGLGVCDI KGAAAALVAA ANASDGDAAF
LFSSDEEAND PRCIAAFLAR GLPYEAVLVA EPTMSEAVLA HRGISSVLMQ FAGRAGHASG
KQDAAASALH QAMRWGNRAL DHVESLASAR FGGLTGLRFN IGRVEGGIKA NMIAPAAEVR
FGFRPLPSMD IDGLLATFAG FAEPEAAVFT ETFRGPSLPA GDIAEAENRR LLARDVADAL
ELPIGNAVDF WTEASLFSAA GYTTLVFGPG DIAQAHTADE FVTLDQLQRY TDAVHRIITA
GA
//
