ID A0A248VKH4_9BURK Unreviewed; 428 AA.
AC A0A248VKH4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:ASV99480.1};
GN Name=argE {ECO:0000313|EMBL:ASV99480.1};
GN ORFNames=CJU94_15805 {ECO:0000313|EMBL:ASV99480.1};
OS Paraburkholderia aromaticivorans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2026199 {ECO:0000313|EMBL:ASV99480.1, ECO:0000313|Proteomes:UP000215158};
RN [1] {ECO:0000313|Proteomes:UP000215158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BN5 {ECO:0000313|Proteomes:UP000215158};
RA Lee Y.;
RT "Identification and genetic characteristics of simultaneous BTEX- and
RT naphthalene-degrading Paraburkholderia sp. BN5 isolated from petroleum-
RT contaminated soil.";
RL Submitted (AUG-2017) 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; CP022989; ASV99480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248VKH4; -.
DR KEGG; parb:CJU94_15805; -.
DR OrthoDB; 3665926at2; -.
DR Proteomes; UP000215158; Chromosome 1.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 210..321
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 45764 MW; 8CFE485DCACFA2AF CRC64;
MSHVADSAQS SQSPDSPSNP ASPASPPAAL PAALPAALPA SLPWVTRLVS MDTVSRNPNL
GLIETVRDEL RAAGIEATLT HDASGKWANL FATIPAHDGE TNGGVVLSGH TDVVPVDGQQ
WDSDPFKPEI RGDKLYGRGT CDMKGFIGAA LALVPEMQRT QLAKPIHFAL SFDEEVGCAG
APLLIADLMK RGVKPDGCIV GEPTSMRPIV AHKGINAYQC CVRGQAAHSS LTPKGLNAIE
YAARLICYIR DMADQFREQG PFDELYDVPF TTAQTSTIVG GNAINTVPAE CRFQFEFRNL
PTLDPEPIFA RIDQYARETL LPKMLREHPS AAIEITKIAA APGLDSSEQA AITQLVRALT
ADQDKRKVAY GTEAGLFSLA GIPSIVCGPG NIEQAHKANE FVALDQLVAC ERFLQKFIHS
MSVGAHAH
//
