ID   A0A1H6WAS9_9BURK        Unreviewed;       819 AA.
AC   A0A1H6WAS9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SEJ09920.1};
GN   ORFNames=SAMN05518853_101630 {ECO:0000313|EMBL:SEJ09920.1};
OS   Variovorax sp. OK202.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1884311 {ECO:0000313|EMBL:SEJ09920.1, ECO:0000313|Proteomes:UP000199192};
RN   [1] {ECO:0000313|EMBL:SEJ09920.1, ECO:0000313|Proteomes:UP000199192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK202 {ECO:0000313|EMBL:SEJ09920.1,
RC   ECO:0000313|Proteomes:UP000199192};
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}.
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; FNZJ01000001; SEJ09920.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6WAS9; -.
DR   Proteomes; UP000199192; 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; 1.10.287.150; -; 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:SF3; ACYL-HOMOSERINE LACTONE ACYLASE PVDQ; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..819
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011570681"
FT   ACT_SITE        274
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         179
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         346
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         349
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   819 AA;  88800 MW;  7D28ECB561F7972F CRC64;
     MTSSLRSIAL ACVTVALAGC AATSTPTAPV GKVTIKRDAY GVPHVYANDV RGLFHGFGYA
     VAEDRLFQME MARRAVLGTV SEVMGPKYVT LDQGSRASFT PDSIRAQMAR LSPDDKAIFD
     GYAAGFNARV KEVLAAPATL LPKEYNDAGF MPKADWTGYD VAMIWVGTMA NRYSNVSSEV
     ANLRLLEQLR KARGDIEGRK LFDQIRWVED PLAPTTVPRT GTTATAAAQL APAGTTAAHA
     AQLAAVSPEL LVARNETDAA RRGVAQPWTR PIASNLWIAG PKKTTDGSTV FINGPQFNWF
     NPSYVFGIGL HGAGFDVTGN TPFAHPVVLF GTNGKIAWGA TAGPLDVNDM YQEKLNPANP
     HEYLFNGAMR PMTQRTEVIK VKGQPDQSVD VYATVHGIVT NFDIPNGTAY SMKRSWDGYE
     LESLLGWIHS MQAQNWDQWL KQASRVAITI NWYYADTSGN IGYVSPGRLP LRPASQDIRL
     PAVGDGSMEW LGIRPFGEDP KTYNPAQGYV ANWNNQSAPG AVSDGGNYSV VDRVREFTAR
     LEAKPKLTPD ELWGLTRTTA YADTNARYIV PFAVEATRNL RPADPARRAA QMLAGWNALN
     EDPAERGVYD SPATTLMMTW LPILYRTVLA DDLPPEVFAA YAGNGYANAT QVASIRPGNG
     LKLVYNALLG PKAGVPQTYD FFNGKDKNAV LRATLTEAMA DLQKRYGSDT AKWRTPVVKH
     AFLTSNFIGA PQASADELLT LPSFMNRGSQ NDKVVLGANG VALCTAAPPG QSGFVAPDGR
     KSAHYADQMT LFKDFGCKSE ALTPADVDRH VESTKQLSY
//