ID A0A418SF77_9RHOB Unreviewed; 388 AA.
AC A0A418SF77;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:QPM89254.1};
DE EC=3.5.1.16 {ECO:0000313|EMBL:QPM89254.1};
GN Name=argE_1 {ECO:0000313|EMBL:QPM89254.1};
GN ORFNames=PSAL_004690 {ECO:0000313|EMBL:QPM89254.1};
OS Pseudooceanicola algae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1537215 {ECO:0000313|EMBL:QPM89254.1, ECO:0000313|Proteomes:UP000283786};
RN [1] {ECO:0000313|EMBL:QPM89254.1, ECO:0000313|Proteomes:UP000283786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lw-13e {ECO:0000313|EMBL:QPM89254.1,
RC ECO:0000313|Proteomes:UP000283786};
RA Poehlein A., Wolter L., Daniel R., Brinkhoff T.;
RT "Genome sequence of Rhodobacteraceae bacterium Lw-13e.";
RL Submitted (AUG-2020) 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; CP060436; QPM89254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418SF77; -.
DR KEGG; palw:PSAL_004690; -.
DR OrthoDB; 9809784at2; -.
DR Proteomes; UP000283786; Chromosome.
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:QPM89254.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000283786}.
FT DOMAIN 173..283
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 388 AA; 42098 MW; 4E87515DAC689D73 CRC64;
MASRLTPFEI MRTLVGFPTV SRDSNLPLID WVQDYLEGHG VTCVRHLHPD QPKAGLWAHV
GPWQDGAVVL SGHTDVVPVD GQEWTDDPFT VIERDGKYFG RGCVDMKSFD ALAIWAMAEA
AGQTLETPLQ LALSYDEELG VIGADPLLRD IEGQVPKGAV AIIGEPTMLK PVTGHKASIA
FDTVVHGFEV HSSLSHTGVS AVMEAARIVD WANSVNAANM AKDPQGSDAL FEPPWTNAHV
GVISGGTAHN ITAKRCEFVI SFRCVPGEDP ESYATLYEAE VRRVEAAMQA IRPEARIELV
GKFRAPGLKP VPDNAAEALA RRLTGDNDTY VVSYGTEAGH FQNHGFAAVV CGPGDIAQAH
QPDEYITIAQ FEAGHDFMRR LLDTLIER
//
