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
//