ID A0A0K0XSE1_9GAMM Unreviewed; 357 AA.
AC A0A0K0XSE1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=HNQ63_002824 {ECO:0000313|EMBL:MBB6088343.1}, WM2015_186
GN {ECO:0000313|EMBL:AKS40575.1};
OS Wenzhouxiangella marina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Wenzhouxiangellaceae; Wenzhouxiangella.
OX NCBI_TaxID=1579979 {ECO:0000313|EMBL:AKS40575.1, ECO:0000313|Proteomes:UP000066624};
RN [1] {ECO:0000313|EMBL:AKS40575.1, ECO:0000313|Proteomes:UP000066624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42284 {ECO:0000313|EMBL:AKS40575.1,
RC ECO:0000313|Proteomes:UP000066624};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB6088343.1, ECO:0000313|Proteomes:UP000581413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103414 {ECO:0000313|EMBL:MBB6088343.1,
RC ECO:0000313|Proteomes:UP000581413};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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; CP012154; AKS40575.1; -; Genomic_DNA.
DR EMBL; JACHIC010000005; MBB6088343.1; -; Genomic_DNA.
DR RefSeq; WP_049724275.1; NZ_JACHIC010000005.1.
DR AlphaFoldDB; A0A0K0XSE1; -.
DR STRING; 1579979.WM2015_186; -.
DR KEGG; wma:WM2015_186; -.
DR PATRIC; fig|1579979.3.peg.191; -.
DR OrthoDB; 3665926at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000066624; Chromosome.
DR Proteomes; UP000581413; 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: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:UP000066624}.
FT DOMAIN 164..265
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 128
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02236"
FT BINDING 70
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02236"
FT BINDING 101
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02236"
FT BINDING 155
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02236"
SQ SEQUENCE 357 AA; 38181 MW; 1AFF1E90DA763643 CRC64;
MERLLHHLAR LVECDSQNPP RAFGPGASMF EHCRQVLEAR GFGVEVADFG DGHVNLYARR
GRPELLFNCH LDTVPVGEGW TRPPLELSVE GDRAYGRGVC DIKGAAAALL TLAEDSDADM
ALLFSSDEEG AGSCCVRRFL ESESHRGYRQ VVVCEPTGCE AILAHRGFLS VKGHFAGVMG
HSSEFRALAD NANHRLARWT TAALAHCESE AAAGRPTCFN LGLVSGGTKS NVIAGDARLH
YSARLGPGQS NEALFDALKD LAGADAHASW EIPFAGPPLP AAGQNDEAAR EFCLAHDLEI
GEPVGFWTEA SLFSAAALPA LVLGPGDIAQ AHAVDEWVEL AQLRQAHEIY ARMIGHG
//
