ID   A0A0M8YIK7_9ACTN        Unreviewed;       914 AA.
AC   A0A0M8YIK7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:KOX29076.1};
GN   ORFNames=ADL06_12985 {ECO:0000313|EMBL:KOX29076.1};
OS   Streptomyces sp. NRRL F-6491.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX29076.1, ECO:0000313|Proteomes:UP000037743};
RN   [1] {ECO:0000313|EMBL:KOX29076.1, ECO:0000313|Proteomes:UP000037743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX29076.1,
RC   ECO:0000313|Proteomes:UP000037743};
RA   Noorani M.;
RL   Submitted (JUL-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:KOX29076.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LGEE01000138; KOX29076.1; -; Genomic_DNA.
DR   RefSeq; WP_053642800.1; NZ_LGEE01000138.1.
DR   AlphaFoldDB; A0A0M8YIK7; -.
DR   PATRIC; fig|1519495.3.peg.2755; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000037743; 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; 2.30.120.10; -; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 2.
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; 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   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2}.
FT   REGION          245..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        311
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         389
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         392
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   914 AA;  99935 MW;  DF275996785CD413 CRC64;
     MPSNTSAPPA KKKGRRARLL LVLLVLVLVA GVGAGGYWGV STVRGSFPQA TGEIRLDSLS
     GQVEVKRDAQ GIPQIYADNE TDLFRAQGYV QAQDRFYEMD VRRHVTAGRL SEMFGEGQVE
     TDSFLRTLGW RRVAQEEYDK VLSAETKKYL QAYAEGVNAY LKDREPGDVS VEYAALALTN
     DYAIEPWTPV DSVAWLKAMA WDLRGNMQDE IDRSLLTSRL TPAQIKQLYP EYPYALHQPI
     VDGGKVDGST GKFDPAGGGD GDDPGTGETP GTDPAGSGDS SQGMSSQLAA LSEVLDGVPA
     LLGPNGNGIG SNSWVVAGKY TTSGKPLLAN DPHLAPQLPS LWYQMGLHCR SVSATCRYDV
     SGYTFSGMPG VIIGHNDKIA WGLTNLGADV TDLYLEKIGP DGYLVDGKVK PFTVREETIK
     VAGGADRKIT VRSTEHGPLV SDRSTELETV GQKAPVGNAA PDRGTGYGVS LQWTALQPGK
     SMDAIFAIDR AKDFDTFRAA ARNFEVPSQN LIYADTEGHI GYQSPGKIPQ RTKGDGTLPA
     PGWDSSYRWK GYIPFEKLPY ELDPERGYIV TANQAVIDPK KYPDLLTKDW GYGSRSQRIN
     DLIESKTKDG GKISPDDMRT MQTDNRSEIA TLLNPLLLKI DIADPHVREA QKLLEGWDYT
     QEPDSAAAAY FNAVWRNVLK LSFGNKLPKE VRAEGDCVNV RPADATGPVD EQNKLVRECG
     QRDPDSAQPD GGDRWYEVVR PLLKQEKSEW WATPGSRTDQ ATETRDQLLA RAMKDARWEL
     TAKLGKDVST WSWGRLHQLT LKNQTLGTAG PGVVQQLLNR GPWNLGGGEA AVDATGWNAA
     GGYEVIWVPS MRMVVNVGDW DKSRWINLTG ASGHAFHSHY TDQTDAWAKG ELYDWAHGRA
     AVDAATKDTL VLKP
//