ID   A0A0R3MEL1_9BRAD        Unreviewed;       425 AA.
AC   A0A0R3MEL1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:KRR16277.1};
DE            EC=3.5.1.16 {ECO:0000313|EMBL:KRR16277.1};
GN   ORFNames=CQ14_33165 {ECO:0000313|EMBL:KRR16277.1};
OS   Bradyrhizobium lablabi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=722472 {ECO:0000313|EMBL:KRR16277.1, ECO:0000313|Proteomes:UP000051660};
RN   [1] {ECO:0000313|EMBL:KRR16277.1, ECO:0000313|Proteomes:UP000051660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCBAU 23086 {ECO:0000313|EMBL:KRR16277.1,
RC   ECO:0000313|Proteomes:UP000051660};
RA   Duran D., Rey L., Navarro A., Busquets A., Imperial J., Ruiz-Argueso T.;
RT   "Bradyrhizobium valentinum sp. nov., isolated from effective nodules of
RT   Lupinus mariae-josephae, a lupine endemic of basic-lime soils in Eastern
RT   Spain.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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:KRR16277.1}.
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DR   EMBL; LLYB01000128; KRR16277.1; -; Genomic_DNA.
DR   RefSeq; WP_057862852.1; NZ_LLYB01000128.1.
DR   AlphaFoldDB; A0A0R3MEL1; -.
DR   STRING; 722472.SAMN05444321_5893; -.
DR   OrthoDB; 9809784at2; -.
DR   Proteomes; UP000051660; 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   CDD; cd03895; M20_ArgE_DapE-like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR010182; ArgE/DapE.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR033687; YodQ-like.
DR   NCBIfam; TIGR01910; DapE-ArgE; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 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   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KRR16277.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          204..316
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   425 AA;  46324 MW;  971721BA1675EC28 CRC64;
     MTTDTQQKIL DAVDAGFEAQ LATTRDFVAI PSTRGAEGPC QDMIGDLLRQ RGYEVDDWHI
     DVEDLKDLRG FGPIEHDFSR ARTVVGTYRP SNNAGKSLIL QGHCDVVPAG PLDMWETPPF
     SPTIKDGRMY GRGACDMKSG TIGALYALDA IKAAGLKPTA RIHFQSVIEE ESTGVGALST
     LQRGYRADAC FIPEPTGETM VRSQVGVIWF RLKVRGFPVH VFEAGAGANA IMAAYHLIHA
     LQKLEADWNE RAKADRHFKA VNHPLNFNPG IIKGGDWASS VPAWCDVDCR IAVLPGWSIA
     ECQKEILACV SAAARDHRFL SNNPPQVEWS GFLSEGYELV NSAEPEAAFA KAFGAVYGGV
     VPDRAFTALT DTRFYGLNHN IPSLCFGAKG AAMHGFNEYV ELDSLRKSTK ATALFIAEWC
     GVEKV
//