ID   A0A1T5EZE0_9SPHI        Unreviewed;       814 AA.
AC   A0A1T5EZE0;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SKB89239.1};
GN   ORFNames=SAMN05661099_3319 {ECO:0000313|EMBL:SKB89239.1};
OS   Daejeonella lutea.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Daejeonella.
OX   NCBI_TaxID=572036 {ECO:0000313|EMBL:SKB89239.1, ECO:0000313|Proteomes:UP000189981};
RN   [1] {ECO:0000313|Proteomes:UP000189981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22385 {ECO:0000313|Proteomes:UP000189981};
RA   Varghese N., Submissions S.;
RL   Submitted (FEB-2017) 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; FUYR01000005; SKB89239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5EZE0; -.
DR   STRING; 572036.SAMN05661099_3319; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000189981; 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:UP000189981};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        277
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         349
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         352
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   814 AA;  92159 MW;  35C4085D0511A940 CRC64;
     MKIIKAVISS LIALTLVISL NSKFGDIPPL GKFMDPFRGF WKNAENSKLN AERDIKIDGL
     RGSVEIKFDE RMVPHIFAEN NYDLYFAQGY ITAKDRLWQM DFQTRFASGR LSEVVGPKAI
     ELDRYQRRMG MTYGAENMVK VMMKDPEIKE TMEAYAAGIN AYIHSLKPGD YPIEFKLLNY
     VPEDWTPLNS ALLLKLMSAT LAGGSNEFYM TNILNKYGPE ITKDLFPDYP FREDPIIPNG
     TKWDFTPVAI PAAPELLSDK KISYQIKTHE IEEGIGSNNW AVSGAKTASG YPLLANDPHL
     DITLPSIWYQ VQVVSPDVNA YGVSIPGAPG VIIGFNQTVA WGVTNVGADV LDWYNIKFKD
     SSKKEYWYNN KWNEVKTRVE TIEVKGGKTI VDSVFYTHHG PIVYTSEQRP DNFSKINNIP
     TGHALRWVAH DGSNDVKTFY KLNRAKNYTD YREALTYYSA PAQNFVFASV ENDIAITPNG
     YFPGKWKGQG KFLMDGSDPA NDWHGRIEAA QNPTVKNPSR NFVSSANQSL TDQTYPYYIN
     WEFAAYERAH RINKRLTVMT KANVDSMINL QNDNYSILAE NILPTLVQLV DTEKLNASER
     EGFDIVSKWN MFFDADEIGA SIFELWHKSL AKEIWEDDLG DPKIPMRYPS RDRNVQLLLN
     EPDSHWFDNV HTAQKETRTD AVNAAFRFTI DSLQRKYGPI DEAWNWGNIK HTNVPHLAKV
     AGFGSKFLKN GGSKSSVNAM SESNGPSWRM VVALGKDVKA YGVFPGGESG NPGSFYYDNM
     IDTWSEGKLN ELLYLKSKED KPKSIHASWT MSKK
//