ID A0A1I2VX73_9SPHI Unreviewed; 810 AA.
AC A0A1I2VX73;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SFG92376.1};
GN ORFNames=SAMN04489864_103248 {ECO:0000313|EMBL:SFG92376.1};
OS Pedobacter insulae.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=414048 {ECO:0000313|EMBL:SFG92376.1, ECO:0000313|Proteomes:UP000199666};
RN [1] {ECO:0000313|EMBL:SFG92376.1, ECO:0000313|Proteomes:UP000199666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18684 {ECO:0000313|EMBL:SFG92376.1,
RC ECO:0000313|Proteomes:UP000199666};
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; FOPP01000003; SFG92376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2VX73; -.
DR STRING; 414048.SAMN04489864_103248; -.
DR OrthoDB; 9759796at2; -.
DR Proteomes; UP000199666; 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:UP000199666};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT ACT_SITE 276
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 810 AA; 92213 MW; 7AC78B95DEC9B05F CRC64;
MNRVKAFICV LIPILLAYTL NTKFGSTPPL LKFLNPFTGF WQNAEGNRQT TKHKIALKGA
KAEINIVFDD RMIPHVFAQN DHDVYYAQGY VTAMHRLWQM DFQTRFAAGR ISEIVGEKAI
EVDRYQRRMG MVYGAENSLK GMMEDPKSKE MILAYTAGIN AYIHSLSRAN YPIEYKILDF
KPEDWTPIKC ALLLKQMSAV LAMGSDEFYM TNILKKFGPE VTKDLFPDYP FKEDPIIPVG
TKWDFKPLSI PDVPKLVTEI MGSTVRTKEK IEGIGSNNWA LSGAKTASGF PLLANDPHLD
LSLPSIWYQI QLHAPGLNTY GVSLPGAPGV TIGFNKDIAW GVTNVAADVL DFYQIKFKDQ
THDQYWYDNA WKKTRKRLEK IQIRGAKTLI DTVYYTHQGP VVYFQKPSYG KASNVPIGSA
LRWIAHDKSN ELMTFYILNR GKNYHDYRKA LTYYTAPAQN FIFASNKNDI AITPNGKFPI
KWKNQGKFVL DGSNPANDWQ GWIPASQNPT VKNPSRNFVS SANQSSTDPN YPYYINWEFS
PYERGKRIND RLTVMNKANV DSMRNLQMDS YSITAQNLLP TILSLVNQAQ LNATQKEAFN
LSAKWNKYFE AKEIAASIFD LWTKRLFYNI WDDEFNIKNI PMRYPSRDRS IELIQNEPNS
TWFDNVKTKE KETLRDLVNE AFKFTCDSLE RKYGPIGKNW EWGNVKNTNV PHLAKIPGFG
TKTLNIGGGK STVNAMSEAN GPSWRMVVEL GKTPKGHGVY PGGQSGNPGS PFYDNMVDTW
AQGKLYDLFF MQSEDDKSGK IISRLKISKK
//