ID J3D081_9BURK Unreviewed; 415 AA.
AC J3D081;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Acetylornithine deacetylase/succinyldiaminopimelate desuccinylase-like deacylase {ECO:0000313|EMBL:EJL82054.1};
GN ORFNames=PMI15_03250 {ECO:0000313|EMBL:EJL82054.1};
OS Polaromonas sp. CF318.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1144318 {ECO:0000313|EMBL:EJL82054.1, ECO:0000313|Proteomes:UP000007275};
RN [1] {ECO:0000313|EMBL:EJL82054.1, ECO:0000313|Proteomes:UP000007275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF318 {ECO:0000313|EMBL:EJL82054.1,
RC ECO:0000313|Proteomes:UP000007275};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:EJL82054.1}.
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DR EMBL; AKIV01000081; EJL82054.1; -; Genomic_DNA.
DR RefSeq; WP_007871105.1; NZ_AKIV01000081.1.
DR AlphaFoldDB; J3D081; -.
DR PATRIC; fig|1144318.3.peg.3140; -.
DR Proteomes; UP000007275; 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; cd03885; M20_CPDG2; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR017150; Pept_M20_glutamate_carboxypep.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF10; BLL3749 PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037238; Carboxypeptidase_G2; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..415
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003763995"
FT DOMAIN 215..312
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 117
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 415 AA; 43652 MW; CB8633495AF8E7D6 CRC64;
MRLNFKGTML ASACSLMLAL VVAVPAAHAQ AMADKAVLEK AESYKGEALA LLEKLVNIDS
GSGYEKGLAQ VRAISVDELK KLGASIETVP SGDGGAHVLA TFLGTGKARI LLMAHMDTVF
KEGTAAAKPF YIKDGRAYGP GVMDNKGGVL AGVYAIKILQ QLQFKDYAKL TFLLDNNEET
GSAIATALIQ KVAKQHDVTL NLEPGRPADG LVIWRKGSGT ATVEVKGKTA HAGVAPELGR
NAAMEAAHQI LQLGKLGSPE KQTTINFTVL KAGDRTNVIP DSASAKADVR VAVPEEFDRI
EKDLARVSAN KLIADTEVKT TLSRGLPPMP QTAHQDALAA KAQAIYGEIG RKLTLEGSGG
AADASLSAGV GVPTLDGFGI VGGNIHTENE YAEVESIVPR FYLLARMVME LSKPN
//
