ID   A0A1H9WZ61_9ACTN        Unreviewed;       842 AA.
AC   A0A1H9WZ61;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SES39196.1};
GN   ORFNames=SAMN04487983_104825 {ECO:0000313|EMBL:SES39196.1};
OS   Streptomyces sp. yr375.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1761906 {ECO:0000313|EMBL:SES39196.1, ECO:0000313|Proteomes:UP000198568};
RN   [1] {ECO:0000313|EMBL:SES39196.1, ECO:0000313|Proteomes:UP000198568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR375 {ECO:0000313|EMBL:SES39196.1,
RC   ECO:0000313|Proteomes:UP000198568};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOFF01000048; SES39196.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9WZ61; -.
DR   STRING; 1761906.SAMN04487983_104825; -.
DR   Proteomes; UP000198568; 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   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; 2.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 2.
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:UP000198568};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   REGION          119..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..736
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        303
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         376
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         379
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   842 AA;  90391 MW;  6E8A4A0EF56D0E8B CRC64;
     MTAEIYRDAW GVPHLRADSA RALARLQGLV TARDRAWQLE VERHRAQGTS ASFLGPEALP
     WDRFVRRARL DDTARRCFDR LERRDPETAD WVRAYVDGVN EGLAEARCAG RASEQAAGRA
     SEQAAGRASE QAAGRASEQA AGRASEQAAG RASEQAAGRA SEQAAGRVPD PASGQTPSQA
     PSQTPAQAPD PASGQAPDPA SGQTPSQAPS QAPSRTPRQA PSQAPRQAPS QTLSQTPSQA
     PEFARVGLVP GGWEAWTPLA VWLATHILFA GFPAKLWREE AARRLGPEAV GLFAADGPGT
     SGSNGWLVSG ARTVTGQPVI AGDPHRFIED PGVYQQIRLA CDEFDVVGLA VPGVPGIAHF
     GHTGTVAWAI TNAMADYQDL YRERLRRTGA GVEALGPDGT WRRVARHTEL VRVAGEETSE
     VEVLETERGP VIAGGPEGLD DGTPDEDDGI PLALSLRYPP RVTADLGFGA LLPLLRARRV
     ADVDRALDLW AEPVNVVQAA DTEGGLLHRV AGRVPLRAAA NGTRLVPAWE PGHEWTGWHE
     TPRAGLTDGV AVMANQRGLS GELGVEFAPP HRADRIGALL AEKRAWTASD MPALHMDTYL
     ASAAPLLDHL TALDDLGDLT TPAAALRDRL LRWDRRMDAD SRDAAGFAAL RSALVRRLAA
     HPAFASLTTP PAYPEVFRPW LALLPRVGFA LEHLLRAEEL YGIDRPALVR EALEEAAGQP
     QSSRQQSAQP SQQRWGDTHR LAPWRALPDA SDQAGPALSG DHDCVLCTSA VPGWTDLAAR
     GPAARYVWDL ARREDSRWVV PYGASGLPGH PHHHDQLPLW LKGELAPVVT DWAHLTKESD
     DD
//