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Database: UniProt
Entry: A0A1G6ZRK5_9PROT
LinkDB: A0A1G6ZRK5_9PROT
Original site: A0A1G6ZRK5_9PROT 
ID   A0A1G6ZRK5_9PROT        Unreviewed;       428 AA.
AC   A0A1G6ZRK5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:SDE05414.1};
GN   ORFNames=SAMN05421720_10314 {ECO:0000313|EMBL:SDE05414.1};
OS   Rhodospira trueperi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospira.
OX   NCBI_TaxID=69960 {ECO:0000313|EMBL:SDE05414.1, ECO:0000313|Proteomes:UP000199412};
RN   [1] {ECO:0000313|EMBL:SDE05414.1, ECO:0000313|Proteomes:UP000199412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700224 {ECO:0000313|EMBL:SDE05414.1,
RC   ECO:0000313|Proteomes:UP000199412};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNAP01000003; SDE05414.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6ZRK5; -.
DR   STRING; 69960.SAMN05421720_10314; -.
DR   OrthoDB; 9809784at2; -.
DR   Proteomes; UP000199412; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199412}.
FT   DOMAIN          206..319
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   428 AA;  46785 MW;  B925C51F2BF68030 CRC64;
     MPALDPTLSR DILSAVDDGF AEQVSFLEDL VRFPSVRGQE HTAQDFMHDA LAARGYAMDR
     WTIDVESIRH HPGFSPVTVD YSHALNVVGS HRPRETAGRS LILNGHMDVV PTGPVDMWAS
     PPFDPRRDGD WLYGRGAGDM KAGLSANVFA VDALRRLGYR PAAPLYQQSV VEEECTGNGA
     LACLARGYRA DAAIIPEPED DKLVRANVGV IWFQVTVRGT PAHVREAGQG ANAIEAAFRL
     IQGLRGLEAD WNARKGDHPH FDHLDAPITF NPGKIAGGDW ASSVPAWCTF DGRFGLYPGV
     SPRDAAREIE ECLRRTAAAD PFMANQPPEV TYNGFMAEGY VLEEGSEAER TLGRAHASAY
     GQSLEAFTTT SYLDGRVFVL YQDTPCLVYG PRAEAIHAFD ERVSLASLRR VTGTIALFIA
     DWCGLERA
//
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