ACDAS_XANCP
ID ACDAS_XANCP Reviewed; 366 AA.
AC Q8P8J5;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=N-acetyl-L-citrulline deacetylase {ECO:0000303|PubMed:16511126, ECO:0000303|PubMed:16750290};
DE Short=ACDase {ECO:0000303|PubMed:16511126};
DE Short=Acetylcitrulline deacetylase {ECO:0000303|PubMed:16511126};
DE EC=3.5.1.- {ECO:0000269|PubMed:16511126, ECO:0000269|PubMed:16585758};
GN Name=argE' {ECO:0000303|PubMed:16511126, ECO:0000303|PubMed:16750290};
GN Synonyms=argE {ECO:0000303|PubMed:16585758, ECO:0000312|EMBL:AAM41525.1};
GN OrderedLocusNames=XCC2246 {ECO:0000312|EMBL:AAM41525.1};
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=16511126; DOI=10.1107/s1744309105018051;
RA Shi D., Yu X., Roth L., Morizono H., Hathout Y., Allewell N.M., Tuchman M.;
RT "Expression, purification, crystallization and preliminary X-ray
RT crystallographic studies of a novel acetylcitrulline deacetylase from
RT Xanthomonas campestris.";
RL Acta Crystallogr. F 61:676-679(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=16585758; DOI=10.1128/jb.188.8.2974-2982.2006;
RA Morizono H., Cabrera-Luque J., Shi D., Gallegos R., Yamaguchi S., Yu X.,
RA Allewell N.M., Malamy M.H., Tuchman M.;
RT "Acetylornithine transcarbamylase: a novel enzyme in arginine
RT biosynthesis.";
RL J. Bacteriol. 188:2974-2982(2006).
RN [4] {ECO:0007744|PDB:2F7V}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP COBALT, COFACTOR, SUBUNIT, DOMAIN, REACTION MECHANISM, ACTIVE SITE, AND
RP 3D-STRUCTURE MODELING.
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=16750290; DOI=10.1016/j.bpc.2006.05.013;
RA Shi D., Yu X., Roth L., Tuchman M., Allewell N.M.;
RT "Structure of a novel N-acetyl-L-citrulline deacetylase from Xanthomonas
RT campestris.";
RL Biophys. Chem. 126:86-93(2007).
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 (PubMed:16585758, PubMed:16511126). Is also able
CC to catalyze the deacetylation of N-acetylornithine in vitro, with
CC almost equal velocity. However, this reaction may be not relevant in
CC vivo since Xanthomonas does not possess the canonical argF gene and
CC cannot convert ornithine to citrulline via ArgF' (PubMed:16585758).
CC {ECO:0000269|PubMed:16511126, ECO:0000269|PubMed:16585758}.
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;
CC Evidence={ECO:0000269|PubMed:16511126, ECO:0000269|PubMed:16585758};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61093;
CC Evidence={ECO:0000305|PubMed:16511126, ECO:0000305|PubMed:16585758};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-acetyl-L-ornithine = acetate + L-ornithine;
CC Xref=Rhea:RHEA:15941, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57805;
CC Evidence={ECO:0000269|PubMed:16585758};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:16750290};
CC Note=Binds 1 Co(2+) ion per subunit. {ECO:0000269|PubMed:16750290};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000305|PubMed:16511126, ECO:0000305|PubMed:16585758}.
CC -!- SUBUNIT: Forms homodimers in the crystal, but higher order oligomers
CC may form in solution. {ECO:0000269|PubMed:16750290}.
CC -!- DOMAIN: Consists of two domains, a catalytic domain (formed by residues
CC 1-166 and 286-365 from the N and C termini, respectively) and a
CC dimerization domain (residues 167-285). {ECO:0000269|PubMed:16750290}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. N-acetylcitrulline
CC deacetylase subfamily. {ECO:0000255|HAMAP-Rule:MF_02236, ECO:0000305}.
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DR EMBL; AE008922; AAM41525.1; -; Genomic_DNA.
DR RefSeq; NP_637601.1; NC_003902.1.
DR RefSeq; WP_011037390.1; NC_003902.1.
DR PDB; 2F7V; X-ray; 1.75 A; A=1-366.
DR PDB; 2F8H; X-ray; 1.75 A; A=1-366.
DR PDBsum; 2F7V; -.
DR PDBsum; 2F8H; -.
DR AlphaFoldDB; Q8P8J5; -.
DR SMR; Q8P8J5; -.
DR STRING; 340.xcc-b100_1933; -.
DR EnsemblBacteria; AAM41525; AAM41525; XCC2246.
DR KEGG; xcc:XCC2246; -.
DR PATRIC; fig|190485.4.peg.2396; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_0_6; -.
DR OMA; YIVGEPT; -.
DR BioCyc; MetaCyc:MON-12074; -.
DR UniPathway; UPA00068; -.
DR EvolutionaryTrace; Q8P8J5; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IBA:GO_Central.
DR GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043909; F:N-acetylcitrulline deacetylase activity; IEA:RHEA.
DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
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 Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Cobalt;
KW Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..366
FT /note="N-acetyl-L-citrulline deacetylase"
FT /id="PRO_0000448223"
FT ACT_SITE 130
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:16750290"
FT BINDING 72
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000269|PubMed:16750290"
FT BINDING 103
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000269|PubMed:16750290"
FT BINDING 155
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000269|PubMed:16750290"
FT HELIX 3..17
FT /evidence="ECO:0007829|PDB:2F7V"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2F7V"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2F7V"
FT TURN 99..104
FT /evidence="ECO:0007829|PDB:2F7V"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2F7V"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:2F7V"
FT HELIX 192..209
FT /evidence="ECO:0007829|PDB:2F7V"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 222..230
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 239..248
FT /evidence="ECO:0007829|PDB:2F7V"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 271..279
FT /evidence="ECO:0007829|PDB:2F7V"
FT HELIX 287..303
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2F7V"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:2F7V"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:2F7V"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:2F7V"
FT HELIX 348..363
FT /evidence="ECO:0007829|PDB:2F7V"
SQ SEQUENCE 366 AA; 38841 MW; 6B4833804602C106 CRC64;
MTDLLASTLE HLETLVSFDT RNPPRAIAAE GGIFDYLRAQ LPGFQVEVID HGDGAVSLYA
VRGTPKYLFN VHLDTVPDSP HWSADPHVMR RTEDRVIGLG VCDIKGAAAA LVAAANAGDG
DAAFLFSSDE EANDPRCIAA FLARGLPYDA VLVAEPTMSE AVLAHRGISS VLMRFAGRAG
HASGKQDPAA SALHQAMRWG GKALDHVESL AHARFGGLTG LRFNIGRVDG GIKANMIAPA
AELRFGFRPL PSMDVDGLLA TFAGFADPAA AHFEETFRGP SLPSGDIARA EERRLAARDV
ADALDLPIGN AVDFWTEASL FSAGGYTALV YGPGDIAQAH TADEFVTLAQ LQRYVESVNR
IINGSH
