ID A0A0D8CL72_9PROT Unreviewed; 428 AA.
AC A0A0D8CL72;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:KJE37035.1};
DE EC=3.5.1.16 {ECO:0000313|EMBL:KJE37035.1};
GN ORFNames=UF64_01470 {ECO:0000313|EMBL:KJE37035.1};
OS Thalassospira sp. HJ.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1616823 {ECO:0000313|EMBL:KJE37035.1, ECO:0000313|Proteomes:UP000032356};
RN [1] {ECO:0000313|EMBL:KJE37035.1, ECO:0000313|Proteomes:UP000032356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HJ {ECO:0000313|EMBL:KJE37035.1,
RC ECO:0000313|Proteomes:UP000032356};
RA Kiseleva L., Garushyants S.K., Goryanin I.;
RT "Complete genome of Thalassospira sp. strain HJ.";
RL Submitted (FEB-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:KJE37035.1}.
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DR EMBL; JYII01000003; KJE37035.1; -; Genomic_DNA.
DR RefSeq; WP_044826836.1; NZ_JYII01000003.1.
DR AlphaFoldDB; A0A0D8CL72; -.
DR STRING; 1616823.UF64_01470; -.
DR PATRIC; fig|1616823.3.peg.3610; -.
DR OrthoDB; 9809784at2; -.
DR Proteomes; UP000032356; 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:KJE37035.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000032356}.
FT DOMAIN 204..313
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 428 AA; 46826 MW; BD79DFE6850CDCBB CRC64;
MSQFDRKSLR EAVSKRTQNA IDDLCALVRH DSQLGSEASA QDWISDKFAA MGLDVERIKI
DINALRDQPG FSPPVIDGYD GRENVVGLHR PQNPTGRSLI LNGHMDVVPT GPAEQWRHGP
FTPHVEDDWI YGRGAGDMKA GIIAYCQALQ ALHDIGLEPA APVTLQSVIE EECTGNGALA
CLHAGYKADC AIIPEPFNQT LMTAQLGVMW FQIHVSGSPA HVLDTSAGSN AIESAFGFFE
TLKEVEEIWN HPTHRHAAFG AHVHPVNFNL GKIEGGEWAS TVPPVCTADI RVGFYPGMEL
EKVRETIEAV KQSALDNHPA CKGAKIEITY RGFQAEGCEM DINHPMMSMI GDIHQEVTGK
EIKKLASTAT TDARFFQIYG NIPATCYGPK AERIHGIDER VSIASMMEVT EVLALFIADW
CGVQKRAS
//
