ID A0A0Q6ARJ6_9BRAD Unreviewed; 425 AA.
AC A0A0Q6ARJ6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:KQT29509.1};
DE EC=3.5.1.16 {ECO:0000313|EMBL:KQT29509.1};
GN ORFNames=ASG57_00700 {ECO:0000313|EMBL:KQT29509.1};
OS Bradyrhizobium sp. Leaf396.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT29509.1, ECO:0000313|Proteomes:UP000051536};
RN [1] {ECO:0000313|EMBL:KQT29509.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT29509.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT29509.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT29509.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQT29509.1}.
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DR EMBL; LMQJ01000001; KQT29509.1; -; Genomic_DNA.
DR RefSeq; WP_057195596.1; NZ_LMQJ01000001.1.
DR AlphaFoldDB; A0A0Q6ARJ6; -.
DR OrthoDB; 9809784at2; -.
DR Proteomes; UP000051536; 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:KQT29509.1};
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; 46223 MW; 331F6E1ECED5588E CRC64;
MNAETQQRIL DAVDSGFEAQ LATTRDFVAI PSTRGAEGPC QDMIGDLLRE RGYEVDDWHI
NVDDLKDLRG FGPIEHDFSK ARSVVGTYRP QTNAGKSLIL QGHCDVVPAG PLELWDTPPF
SPVIKDGKMF GRGACDMKSG TIGALYALDA IKAAGLRPTA RIHFQSVIEE ESTGVGALST
LQRGYRADAC FIPEPTGGKM VRSQVGVIWF RLRVKGHPTH VAFAGSGANA IMAAYHLIQA
LQKLEIEWNE RAKADRHFKT LNHPINFNPG IIKGGDWASS VPAWCDVDCR IAVLPGWSIA
DHQKEITACV AAAARNHRFL ANNPPEIEWS GFLSEGYELT DAAAPETAFG KAFNAVYGGA
VEDLVFTALT DTRFYGLNHG IPSLCFGASG GEMHGFNEFV DLESLRKTTK AMALFIAEWC
GVEKA
//
