ID   A1WN00_VEREI            Unreviewed;       782 AA.
AC   A1WN00;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:ABM59007.1};
DE            EC=3.5.1.11 {ECO:0000313|EMBL:ABM59007.1};
GN   OrderedLocusNames=Veis_3277 {ECO:0000313|EMBL:ABM59007.1};
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735 {ECO:0000313|EMBL:ABM59007.1, ECO:0000313|Proteomes:UP000000374};
RN   [1] {ECO:0000313|Proteomes:UP000000374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2 {ECO:0000313|Proteomes:UP000000374};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL   Submitted (DEC-2006) 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; CP000542; ABM59007.1; -; Genomic_DNA.
DR   RefSeq; WP_011810999.1; NC_008786.1.
DR   AlphaFoldDB; A1WN00; -.
DR   STRING; 391735.Veis_3277; -.
DR   MEROPS; S45.003; -.
DR   GeneID; 76461724; -.
DR   KEGG; vei:Veis_3277; -.
DR   eggNOG; COG2366; Bacteria.
DR   HOGENOM; CLU_011790_0_0_4; -.
DR   OrthoDB; 9760084at2; -.
DR   Proteomes; UP000000374; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008953; F:penicillin amidase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:ABM59007.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000374};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..782
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002640731"
FT   ACT_SITE        261
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         333
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         336
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   782 AA;  87092 MW;  6D08466F14E2DF28 CRC64;
     MATLKSCALA LLACSAISSH AATQTLHVPG LQKKAEILID KWGVPHIYAA SQTDAFFVQG
     FNAARDRLFQ IDLWRRRGLG QLSEVFGPAY IAQDQATRLF LYRGDMQREW DSYGKQSEQI
     ATAFVAGINA YIDLVTAHPE RLPYEFKQLA YQPAKWQAED VVRIRSHGLT RNLNSEVARA
     NVVCKADLKS DEIRFGLQPK WQAVMPEGLD PCLPKDLLKV FQLATQNVRI TKESLSAHAD
     GQGDGIRIAA AENPEESTEG SNNWVIAPAK SATGRAIMAN DPHRAYSAPS LRYIAHLNAP
     GLHVIGAGEP ALPGISIGHN GTIAFGLTIF SIDQEDLYVY ELNPDNPDEY KYQGKWEPFQ
     VLHEPIRVKG GVPETADLRF TRHGPVIFAD RQRAFAVRSC WLEPGMSPYF GSIGYMHAKS
     FNSFKRAIVN WDAPTVNLVY ADVKGNIGWA PGGLAPKRPN WDGLMPVPGD GRYEWAGFWS
     GDQLPRVYNP RQGWFATANQ MNLPEDYPYR ERRLGFEWTN GSRFMRISEV LSSLPKVTLQ
     DAMRLQNDDL AIPARRLVAL LKLDAGTPAA IFKGWDYVER VDSPQAALYE VWLARHLGKA
     FKEAVLSKEA AAAMGAPDVA VMLNMLEQPG AVPGRDELLR DSLRDAYAEM VKLQGEDASQ
     WQWGKLHHNL MEHPLAAVVD EEMRARLNVG PLPKRGGAYG PNQSTYRASD FRQTNGPSFR
     VVVDVGHWDG SVAINAPGQS GDPNSPHYRD LTERWLDGEY FPLLYSRKAV EQATVQRIVL
     KP
//