ID A0A103E6X3_9BURK Unreviewed; 405 AA.
AC A0A103E6X3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:KVE29507.1};
DE EC=3.5.1.16 {ECO:0000313|EMBL:SMF98430.1};
GN ORFNames=BSIN_1715 {ECO:0000313|EMBL:SMF98430.1}, WS67_04860
GN {ECO:0000313|EMBL:KVE29507.1};
OS Burkholderia singularis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=1503053 {ECO:0000313|EMBL:KVE29507.1, ECO:0000313|Proteomes:UP000062788};
RN [1] {ECO:0000313|EMBL:KVE29507.1, ECO:0000313|Proteomes:UP000062788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSV85 {ECO:0000313|EMBL:KVE29507.1,
RC ECO:0000313|Proteomes:UP000062788};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SMF98430.1, ECO:0000313|Proteomes:UP000198460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 28154 {ECO:0000313|EMBL:SMF98430.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; LOWA01000013; KVE29507.1; -; Genomic_DNA.
DR EMBL; FXAN01000025; SMF98430.1; -; Genomic_DNA.
DR RefSeq; WP_059513452.1; NZ_LOWA01000013.1.
DR AlphaFoldDB; A0A103E6X3; -.
DR OrthoDB; 3665926at2; -.
DR Proteomes; UP000062788; Unassembled WGS sequence.
DR Proteomes; UP000198460; 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, ECO:0000313|EMBL:SMF98430.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000062788}.
FT DOMAIN 191..301
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 405 AA; 43529 MW; B4AF0EC351880944 CRC64;
MSFVDATAPS AAASPSRAEP ISLDWTRRLV SIDTTSRVPN LGLIEMVRDA LANAGVTSTL
THDARDGWAN LFATLPAHDG STHGGIVLSG HTDVVPVDGQ QWDSDPFRPE VRDGKLYGRG
TCDMKGFIGA ALALLPEMRA AKLAQPIHFA LSYDEEIGCA GAPLMLADLK SRGIAPAGCI
VGEPTGMRPV IAHKGVNVYR CCVRGHAAHS SLTPKGLNAI EYAARLICRI RDIADEFRAQ
GPFDALYDVP FSTAQTSLIK GGNAVNTVPA ECEFSFEFRN LPTLDPDAIF ARIDAYARDT
LLPLMRREHP NAAIEFSKVA AAPGLDAAEQ EAITQLVRSL TADQEKRKVA YGTEAGLFQR
AGIPSVVCGP GYIEQAHKPN EYVELDQLAS CERFLRKLVH GLTLA
//
