ID H0E893_9ACTN Unreviewed; 371 AA.
AC H0E893;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:EHN10094.1};
DE EC=3.5.1.16 {ECO:0000313|EMBL:EHN10094.1};
GN ORFNames=PAI11_30540 {ECO:0000313|EMBL:EHN10094.1};
OS Patulibacter medicamentivorans.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Patulibacteraceae; Patulibacter.
OX NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN10094.1, ECO:0000313|Proteomes:UP000005143};
RN [1] {ECO:0000313|EMBL:EHN10094.1, ECO:0000313|Proteomes:UP000005143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I11 {ECO:0000313|EMBL:EHN10094.1,
RC ECO:0000313|Proteomes:UP000005143};
RX PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT strain I11.";
RL Biodegradation 24:615-630(2013).
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:EHN10094.1}.
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DR EMBL; AGUD01000241; EHN10094.1; -; Genomic_DNA.
DR RefSeq; WP_007576734.1; NZ_AGUD01000241.1.
DR AlphaFoldDB; H0E893; -.
DR PATRIC; fig|1097667.3.peg.3027; -.
DR OrthoDB; 9783294at2; -.
DR Proteomes; UP000005143; Unassembled WGS sequence.
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; 1.
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:SF17; BLL2699 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:0000313|EMBL:EHN10094.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005143}.
FT DOMAIN 184..267
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 371 AA; 38029 MW; B16D94564DD2C6EC CRC64;
MLASLDPLVE QIVATTLELT AVPAPTGDEG DRAAVVGRRL ADLGLPVEHD EVGNVVSRLP
LAGGRVPPVD APALVVSAHL DTVFGRDVAL EPRRDGERLL GPGIGDDTVA LAALLALAGE
LAASPPPTPV VLAATVGEEG LGDLRGAKHL LRSVPTRAFV AVEGHLLDDL VTGGIGALRL
CATYRGSGGH SWGDRGAASA AHALLVAGAA ALKAVPAGRH VNVGVIEAGT TVNAIAAEAR
LLVDLRDEDD GRLRRTATLV RRALEAAPRG IHATVEQVGH RPAGQTPRDH PLLRAARAAR
ADVGLPRARE DSGSTECNAA FPLGIPTVCV GITRGADMHR TSEWVAIPPI ADGIAALRAL
VRRASAEDSG V
//
