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Database: UniProt
Entry: A0A1G9V4N1_9BACT
LinkDB: A0A1G9V4N1_9BACT
Original site: A0A1G9V4N1_9BACT 
ID   A0A1G9V4N1_9BACT        Unreviewed;       811 AA.
AC   A0A1G9V4N1;
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:SDM67142.1};
GN   ORFNames=SAMN04488090_3962 {ECO:0000313|EMBL:SDM67142.1};
OS   Siphonobacter aquaeclarae.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC   Siphonobacter.
OX   NCBI_TaxID=563176 {ECO:0000313|EMBL:SDM67142.1, ECO:0000313|Proteomes:UP000198901};
RN   [1] {ECO:0000313|EMBL:SDM67142.1, ECO:0000313|Proteomes:UP000198901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21668 {ECO:0000313|EMBL:SDM67142.1,
RC   ECO:0000313|Proteomes:UP000198901};
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; FNGS01000008; SDM67142.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9V4N1; -.
DR   STRING; 563176.SAMN04488090_3962; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000198901; 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:UP000198901};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        278
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         350
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         353
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   811 AA;  91397 MW;  C08B8178A83198ED CRC64;
     MVKAVLSVAV TGGLLWLLST PLGPAPALGS FLSPFTGFWS NERRVDMLNE EIHLPGAQEE
     ITIRFDDNRV PHIFAANDHD LYYAQGYVTA RDRLFQMELT IRSAAGRLSE IVGEKALPLD
     LYKRRTGSVK AAEEAWKFTQ QDEKMRGILE AYSDGVNAYI SQLRKADYPV EYKLLGFQPE
     AWSPEKSMLL MVEMTHTLAS PRSGDASLTS VLEKFGLEVV RDLYPDFVER ESPVIPKGTA
     WDFRRVAIPR APRDYDEIKA GGASEPDSWP LRPEGIGSNN WAVSGKKSAT GFPILAGDPH
     LGLTLPSIWY QVQLSSPESN ACGASLPGAP CVIIGFNRDV AWSETNVASD VADLYAIRFR
     DKSRKEYFFD KQWVKTTFRY EEIKIKGKPA VIDTVAYTHH GPVAMPRFPE DKQPSLALRW
     IAHEPGNPIR TFYMLNRAKN YDDYVRALSH YVSPAQNFVF ASNEGDIAIW VNGKFPLKWK
     EQGKFLLDGT RPEYDWQGWI PHEQNPHVKN PASGYVSSAN QSSTDKTYPY YLNWRFAPPN
     RAIRINERLA AMEQATPDSL RLLQNDVYNV LGRDLLPDLL KELDMSALSA TQYSAYSALQ
     QWNYQNTIGS VGATIFEEWT DLLPYFVWDE FRTTDGKPLQ APQDDRVWEL IWKKKESKWF
     DLEKTTDKTE TARDIIQLSF KAAVDSLQKH HGAFSPKTWA WGEVKGSTIA HLLPPLKSFG
     RDDVRAGGSS EVPNAFRGKW GPSWRMVVAL GKDGPTAYGV YPGGQSGNPG SPFYDNMVNT
     WRDGRLNELV YLKSGAEPNP RIVGTWKITK P
//
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