ID H6RMF4_BLASD Unreviewed; 397 AA.
AC H6RMF4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:CCG02590.1};
DE EC=3.5.1.16 {ECO:0000313|EMBL:CCG02590.1};
GN Name=argE {ECO:0000313|EMBL:CCG02590.1};
GN OrderedLocusNames=BLASA_1667 {ECO:0000313|EMBL:CCG02590.1};
OS Blastococcus saxobsidens (strain DD2).
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG02590.1, ECO:0000313|Proteomes:UP000007517};
RN [1] {ECO:0000313|EMBL:CCG02590.1, ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|EMBL:CCG02590.1,
RC ECO:0000313|Proteomes:UP000007517};
RX PubMed=22535935; DOI=10.1128/JB.00320-12;
RA Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA Gury J., Pujic P., Normand P.;
RT "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT Bacterium.";
RL J. Bacteriol. 194:2752-2753(2012).
RN [2] {ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA Genoscope.;
RT "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL Submitted (FEB-2012) 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; FO117623; CCG02590.1; -; Genomic_DNA.
DR RefSeq; WP_014375482.1; NC_016943.1.
DR AlphaFoldDB; H6RMF4; -.
DR STRING; 1146883.BLASA_1667; -.
DR KEGG; bsd:BLASA_1667; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_0_11; -.
DR OrthoDB; 7055905at2; -.
DR Proteomes; UP000007517; Chromosome.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
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 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.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 4: Predicted;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCG02590.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007517};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 188..291
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 41490 MW; C05D8A895FE9A01F CRC64;
MTKLPDTAGL SPTTQPVDGD PEVIRLLKEL VTIESVNPAL DPTGAGEGPL AAYIHQWATE
RGLTARVEDD GSGRPNVIVE SRPPAPGIPT LLLCGHLDTV SLASVTDPLL PRVEGDRLYG
RGTYDMKAGL AASLVACQRA HEADLPVSVV VAGVADEEHA SLGAQRLVEN LQADAAIVCE
PTEMTVGIAH KGFVWTDIEV HGLAAHGSRP ELGVDAIVKT GPILVELERL TESLKSRVHP
LLGPASVHAS VISGGVEAST IPDRCLLTIE RRTLPDESVA DVEAELAALL QACRDADSQL
NVTARTVLHR PPMQTSPDEH LVAVVGDAIR DALGVEAEVV GMSYWADSAF ISALGIPTVL
LGPSGEGAHA EVEWVSISET IACADVLYTA AEALAAA
//
