ID   A0A1H3RBE1_9RHOB        Unreviewed;       819 AA.
AC   A0A1H3RBE1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SDZ22833.1};
GN   ORFNames=SAMN05444004_10840 {ECO:0000313|EMBL:SDZ22833.1};
OS   Jannaschia faecimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=1244108 {ECO:0000313|EMBL:SDZ22833.1, ECO:0000313|Proteomes:UP000198914};
RN   [1] {ECO:0000313|EMBL:SDZ22833.1, ECO:0000313|Proteomes:UP000198914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100420 {ECO:0000313|EMBL:SDZ22833.1,
RC   ECO:0000313|Proteomes:UP000198914};
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; FNPX01000008; SDZ22833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3RBE1; -.
DR   STRING; 1244108.SAMN05444004_10840; -.
DR   OrthoDB; 9760084at2; -.
DR   Proteomes; UP000198914; 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   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        260
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         195
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         332
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         335
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         520
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   819 AA;  89868 MW;  50AAE8BE37C1120B CRC64;
     MERLFRWTFR IVTAALLLAG LSVLAVYWLA GRSLPDYDAT ETVAGLSAPV EIVRNTHNVP
     HIFGETDADV FFGLGYAHAQ DRLWQMTLLR RTAQGKLSEI FGQRTVRTDE LLLRLGLYRA
     AVRSVDALDS ESLAMLEAYA RGVNARIKVI NAEASGRGAP EFFLFSPQVA PWQPADSLAI
     VKLMALQLSG HVEEEVLRAR ASLVLEEARL RDLHPDLPGD GKVVLAGDLF PSLRSRQFAD
     ADKRDPFLWP VPPRDLAGAS NAFAVAPDRA AAGGALLAND PHLGLTAPTL WYLARLELTT
     GGAIGGTIPG MPIILLGRTA RLGWGLTSAY MDDQDVMIEQ LNPEDSTQYR TPDGWADFET
     ERTIVTIKDA EPITLTLRRT VNGPVLTGRQ FDLGTVTPQG HVAALAWTAL AEDDTSMRTG
     LELMRAGDVE AGLAAARHFV APAQNLMLTD GDRIAITIMG RQPDRNELQQ SEGRIPVPGW
     IAVNHWGGLK PADSNPVWAD PDGGLLGNTN NKTTDAFFPD HISHWWGDSQ RVQRMERLMQ
     ARSVHTRESL IEAQLDTVST AARSLLPLIG RDLWFTGDAA PAGTPERRRQ VALELLAAWN
     GEMSEHLPEP LIYAAWMRSL QQRLIRDDLG PLAAEYPRME PLFVERVFRD IGGASAWCDV
     IQSTQPETCT DIARQSLDDA LQFLEDTYGA RVETWRWGDA HQARSDHTVL GDIPILGLVV
     NIRQSTSGGD HTLQRGRTGG ALPAPFLNVH AATYRGVYDF ADPESSVFIT STGQSGHPLS
     KHYDDLGELW RRGEYIPMTL DPELARAGAV GVTVLNPAR
//