ID A0A1M5BKY0_9BACT Unreviewed; 817 AA.
AC A0A1M5BKY0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SHF43096.1};
GN ORFNames=SAMN02745131_02629 {ECO:0000313|EMBL:SHF43096.1};
OS Flavisolibacter ginsengisoli DSM 18119.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavisolibacter.
OX NCBI_TaxID=1121884 {ECO:0000313|EMBL:SHF43096.1, ECO:0000313|Proteomes:UP000184048};
RN [1] {ECO:0000313|EMBL:SHF43096.1, ECO:0000313|Proteomes:UP000184048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18119 {ECO:0000313|EMBL:SHF43096.1,
RC ECO:0000313|Proteomes:UP000184048};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQUU01000010; SHF43096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5BKY0; -.
DR STRING; 1121884.SAMN02745131_02629; -.
DR Proteomes; UP000184048; 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 Reference proteome {ECO:0000313|Proteomes:UP000184048};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT ACT_SITE 287
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 359
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 817 AA; 92908 MW; 6FCEC91BFC3A1451 CRC64;
MLMRIIPFVI SLVVTLGLVF ALNTKIGTIP PLGKFLSPQQ GFWQNAEPCD ARLDEDLRFP
DLKGKVKVYM DERMVPHVFA ENDEDVYFVQ GYLHAKYRLF QMEFQTHAAA GRLSEILGNN
PQIINYDRLQ RRMGMVYGAE NELKAVAKDA LTQKVYDAYT AGVNSYINSL SAGNLPVEYK
LLDFRPEPWT NLKIALFFKV MCSDLAGQEY AKDISFSNEK SLFSKEEMDM LYPQVSDSSV
SIIPKGTIFE SPSVHPEIPA NADSFYLQKD SIAEPVKVPK PFEVKGSNNW VVSGAKTKSG
APILCNDPHL RLTLPSIWYE MQLHTPTMNV YGVGFPSVPG IVIGYNDSIA IGLTNAGRDV
MDYYQVKFKD ASRNEYWYKN QWQAAEHRIE KIKVKGGATI IDTVAYTVFG PVTYDRSFTT
ADSNTNKALA MRWTAHDPSN EVLTLIKLNR AKNYSEYSQA IKEFACPGQN IIFGSTNGDI
AIWQQGKFPA RWKNQGLYVM PGEDDTYSWQ GFIPQGENPH VLNPPDNFLQ SANQRAVDSS
YPYFIPGDYY VPRGRSIYRQ LSQMQDITPQ DMMRLQGNAY STLAGDAMPL FSKYLKTNEL
SDNELKYWEE VSKWNFEYTG QERAPTIFQT WMDSLESVIW SDEFTQASKP VTIPSEQILL
ENLLRDSAFR FVDNINTPEK ENLYQDVTLS FKKAVGELVK NEDGVIWWKH RNTFIQHLLR
DALPAFGRTG LMCNGWSTTI NALTKTHGPS WRMVIHLTKP IEAYGVYPGG QSGNPGSKFY
ENFIDTWATG KYFTLWMMHE NESSDKRIIG QINFTNS
//