ID I4MZ65_9PSED Unreviewed; 384 AA.
AC I4MZ65;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:EIK94505.1};
DE EC=3.5.1.16 {ECO:0000313|EMBL:EIK94505.1};
GN ORFNames=PMM47T1_21478 {ECO:0000313|EMBL:EIK94505.1};
OS Pseudomonas sp. M47T1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK94505.1, ECO:0000313|Proteomes:UP000004339};
RN [1] {ECO:0000313|EMBL:EIK94505.1, ECO:0000313|Proteomes:UP000004339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M47T1 {ECO:0000313|EMBL:EIK94505.1,
RC ECO:0000313|Proteomes:UP000004339};
RX PubMed=22887683; DOI=10.1128/JB.01116-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL J. Bacteriol. 194:4789-4790(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.
CC {ECO:0000256|ARBA:ARBA00005691}.
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:EIK94505.1}.
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DR EMBL; AJWX01000023; EIK94505.1; -; Genomic_DNA.
DR RefSeq; WP_008372875.1; NZ_AJWX01000023.1.
DR AlphaFoldDB; I4MZ65; -.
DR STRING; 1179778.PMM47T1_21478; -.
DR MEROPS; M20.974; -.
DR PATRIC; fig|1179778.3.peg.4291; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 3665926at2; -.
DR Proteomes; UP000004339; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR CDD; cd03894; M20_ArgE; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_01108; ArgE; 1.
DR InterPro; IPR010169; AcOrn-deacetyl.
DR InterPro; IPR001261; ArgE/DapE_CS.
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:SF1; ACETYLORNITHINE DEACETYLASE; 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.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EIK94505.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000004339};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 175..282
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 384 AA; 41701 MW; 08B47CFC7F7F0714 CRC64;
MPLPSFKEQF AALIAAPSVS CTQASLDQSN KPVIDLLASW LGDLGFACDI REVLPGKFNL
LASRGTGPGG LVLSGHSDTV PYDEKLWQTD PLKLTEVDGR WVGLGSCDMK GFFALIIEAV
LPLLAHDFKQ PLLILATCDE ESSMAGAKAL AAAGWPLGRA AVIGEPTGLK PIRLHKGVMM
ERIDILGRSG HSSDPSLGHS AMEAMHGAIS ELMGLRKQWQ VEYNNPQFSV PQPTLNFGCI
HGGDNPNRIC GQCSLEFDLR PLPGMDPKAL RAAIRQKLEP LAELHQVKID YAPLFSEVPP
FEQSADSELV RVAERLTGHR AEAVAFGTEA PYLQRLGCET LILGPGDIAC AHQPGEFLEM
SRLEPTVRLL RELIEYYCLQ PVGH
//
