ID   A2W9I0_9BURK            Unreviewed;       406 AA.
AC   A2W9I0; A0A0D5J2F8;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:EAY68626.1};
GN   ORFNames=BDAG_01351 {ECO:0000313|EMBL:EAY68626.1};
OS   Burkholderia dolosa AU0158.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=350701 {ECO:0000313|EMBL:EAY68626.1, ECO:0000313|Proteomes:UP000053482};
RN   [1] {ECO:0000313|Proteomes:UP000053482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU0158 {ECO:0000313|Proteomes:UP000053482};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA   Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E., Brockman W., Rounsley S., Young S., LaButti K., Pushparaj V.,
RA   DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA   Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., Oleary S.,
RA   Alvarado L., Lory S., LiPuma J.;
RT   "The Genome Sequence of Burkholderia dolosa (strain AU0158).";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; CH482380; EAY68626.1; -; Genomic_DNA.
DR   RefSeq; WP_006764099.1; NZ_CP009795.1.
DR   AlphaFoldDB; A2W9I0; -.
DR   GeneID; 64460939; -.
DR   PATRIC; fig|350701.8.peg.1280; -.
DR   HOGENOM; CLU_021802_2_4_4; -.
DR   OrthoDB; 3665926at2; -.
DR   Proteomes; UP000053482; Unassembled WGS sequence.
DR   GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:InterPro.
DR   CDD; cd03894; M20_ArgE; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR010169; AcOrn-deacetyl.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01892; AcOrn-deacetyl; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 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   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          190..301
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   406 AA;  43847 MW;  66F58847476E11C9 CRC64;
     MSTLDATAQS AADQRDASPV SLPWVKQLVS MDTTSRVPNL GLIETVRDAL AAKGITSTLT
     HDPREGWANL FATVPAHDGS TDGGIVLSGH TDVVPVDGQQ WDSDPFAPEV RDDRLYGRGT
     CDMKGFIGAA LALLPEMQAT KLAKPIHFAL SYDEEIGCAG APLMIADLVK RGVKPSGCIV
     GEPTSMRPII AHKGINAYRC CVRGHAAHSS LTPKGLNAIE YAARLICHIR DIAERFRADG
     PFDELYDVPF TTAQTSTIQG GNAINTVPAE CRFDFEFRNL PTLDPDQIFA RIEAYAQETL
     LPQMLREHPN AAIEFSKIAA APGLDATEQA AITQLVRALT ADQDKRKVAY GTEAGLFQRA
     GIPSVVCGPG NIEQAHKPNE YVELAQLAGC EQFLRKFIRS MSVDAH
//