ID   A0A0Q8VIW5_9ACTN        Unreviewed;       859 AA.
AC   A0A0Q8VIW5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:KRC53810.1};
GN   ORFNames=ASE19_06885 {ECO:0000313|EMBL:KRC53810.1};
OS   Nocardioides sp. Root79.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736600 {ECO:0000313|EMBL:KRC53810.1, ECO:0000313|Proteomes:UP000051414};
RN   [1] {ECO:0000313|EMBL:KRC53810.1, ECO:0000313|Proteomes:UP000051414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root79 {ECO:0000313|EMBL:KRC53810.1,
RC   ECO:0000313|Proteomes:UP000051414};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC53810.1, ECO:0000313|Proteomes:UP000051414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root79 {ECO:0000313|EMBL:KRC53810.1,
RC   ECO:0000313|Proteomes:UP000051414};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001227-2};
CC       Note=Binds 1 Ca(2+) ion per dimer. {ECO:0000256|PIRSR:PIRSR001227-2};
CC   -!- SIMILARITY: Belongs to the peptidase S45 family.
CC       {ECO:0000256|ARBA:ARBA00006586}.
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:KRC53810.1}.
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DR   EMBL; LMIP01000010; KRC53810.1; -; Genomic_DNA.
DR   RefSeq; WP_056895241.1; NZ_LMIP01000010.1.
DR   AlphaFoldDB; A0A0Q8VIW5; -.
DR   Proteomes; UP000051414; Unassembled WGS sequence.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   CDD; cd03747; Ntn_PGA_like; 1.
DR   Gene3D; 1.10.1400.10; -; 1.
DR   Gene3D; 2.30.120.10; -; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   Gene3D; 1.10.439.10; Penicillin Amidohydrolase, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR014395; Pen/GL7ACA/AHL_acylase.
DR   InterPro; IPR043147; Penicillin_amidase_A-knob.
DR   InterPro; IPR023343; Penicillin_amidase_dom1.
DR   InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR   InterPro; IPR002692; S45.
DR   PANTHER; PTHR34218:SF4; ACYL-HOMOSERINE LACTONE ACYLASE QUIP; 1.
DR   PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR   Pfam; PF01804; Penicil_amidase; 1.
DR   PIRSF; PIRSF001227; Pen_acylase; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051414};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   REGION          223..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        279
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         190
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         357
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         360
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   859 AA;  93230 MW;  C10CAC916945A31A CRC64;
     MAGIAVLLVL ALVAGVVTAV VMVRRPWPET SGELELSGLE GEVRVVRDDA GIPQVYADSM
     HDLMLAQGFV HAQDRFFEMD VRRHATAGRL SELFGEDGLE SDLVVRTLGW RRVAEQELTM
     LRPATRSALD AYAEGVNAYL AGRSTSEMAL EYSLLGISGL DYTPEKWSAV DSIAWLKAMA
     WDLRGNLDEE IGRALTTATV GARATEELYP SYPFGEHPPI VDQGGLRGEE FDQDATSGDG
     GPLQRPAPGG HRAVAALAGV RDVLAGVPAL LGKGDGIGSN SWVVDGDHTS TGWPILANDP
     HLGISLPGVW AQVGLHCREV TPDCPMDVSG FSFSGVPGVV IGHNADIAWG FTNLGADVTD
     LYVERVADDT WQYDGRTRAL DVRDERIEVR DGDPVDITVR STDHGPLLSD LTAVDERLDE
     VDLTTDGLVD EVDQVGDAEE DTDSAWETGV SLAWTALEPH PTADALLALD TADDWPSFRA
     ALRSFAAPGQ NVVYADTQGH IGYQATGLVP IRRAGNDGRT PAAGWRADTG WTGRHVPYDA
     LPNVLDPASG IIATANQAVI DPRRYPPFLT EDWDQGYRST RINQLLAADD ELSVDQMGSI
     QLDDWSAIAE VLTPYLLKVG LPHGYYSDGQ RLLRSWNHRQ GADSAAAAYF NVVWREVLER
     TFADELPDVL EPDGSDRWFA VVASILPRTA NHWWDDVETD DQVEDRDDVL REAMIAARDE
     LTARESPNAD EWTWGALHEL ELRSATLGES GIGPVEWLFN RGPWEVGGGG SLVDATAWDA
     REGYDVTTAP SMRMVVPMDD LDAARWINLT GASGHAFNPH YTDQTDLWAR GETLPWAFSA
     DAVEDAADDV LVLTDGSAG
//