ID A0A154R052_9GAMM Unreviewed; 377 AA.
AC A0A154R052;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=RhoFW510R10_16800 {ECO:0000313|EMBL:KZC31414.1};
OS Rhodanobacter sp. FW510-R10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1524462 {ECO:0000313|EMBL:KZC31414.1, ECO:0000313|Proteomes:UP000076310};
RN [1] {ECO:0000313|EMBL:KZC31414.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW510-R10 {ECO:0000313|EMBL:KZC31414.1};
RX PubMed=27048805; DOI=10.1128/mBio.02234-15;
RA Hemme C.L., Green S.J., Rishishwar L., Prakash O., Pettenato A.,
RA Chakraborty R., Deutschbauer A.M., Van Nostrand J.D., Wu L., He Z.,
RA Jordan I.K., Hazen T.C., Arkin A.P., Kostka J.E., Zhou J.;
RT "Lateral Gene Transfer in a Heavy Metal-Contaminated-Groundwater Microbial
RT Community.";
RL MBio 7:e02234-e02215(2016).
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:KZC31414.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LVJU01000027; KZC31414.1; -; Genomic_DNA.
DR RefSeq; WP_068097712.1; NZ_LVJU01000027.1.
DR AlphaFoldDB; A0A154R052; -.
DR OrthoDB; 3665926at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000076310; 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}.
FT DOMAIN 163..267
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 377 AA; 40039 MW; 665116B3CE0E11B3 CRC64;
MSDLLQSTLE HLKALVSFDT RNPPRAITTG GIFDYIRAHL PGFDVAVTDH GAGAVGLHAM
RGQPKLLFNV HLDTVPDSPA WTASPHELRV TTDRAIGLGA CDIKGAAAAL LAVANAGSGD
MALLFTTDEE ANDPRCIAGF LADKPAYDAV IVAEPTKGEA VLAHRGIQSV LMRFAGHAGH
ASGEQKPGDS ALHQAVRWGD AALDFVAAQA HERFGGLTGL RFNIGRIEGG IKANMIAPSA
EVRFGMRPLP TMHPDGLLER FRTLVEPMPA EFAETFRGPS LPAGDTATAE ARRLAARDLA
DELGIPVGNA VDFWTEAALF SAAGYTAFVY GPGDIAQAHS ADEWVALDQL QHYAEVAFRL
VEKCGQGRPL FDSRVHG
//
