ID A0A0F7JUJ0_9DEIO Unreviewed; 782 AA.
AC A0A0F7JUJ0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Penicillin amidase {ECO:0000313|EMBL:AKH18440.1};
GN ORFNames=SY84_08590 {ECO:0000313|EMBL:AKH18440.1};
OS Deinococcus soli (ex Cha et al. 2016).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1309411 {ECO:0000313|EMBL:AKH18440.1, ECO:0000313|Proteomes:UP000034024};
RN [1] {ECO:0000313|EMBL:AKH18440.1, ECO:0000313|Proteomes:UP000034024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N5 {ECO:0000313|EMBL:AKH18440.1,
RC ECO:0000313|Proteomes:UP000034024};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Deinococcus soli/N5/whole genome sequencing.";
RL Submitted (JAN-2015) 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; CP011389; AKH18440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7JUJ0; -.
DR KEGG; dch:SY84_08590; -.
DR PATRIC; fig|1309411.5.peg.1754; -.
DR Proteomes; UP000034024; Chromosome.
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:UP000034024};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT REGION 211..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 782 AA; 83962 MW; 90635BDA4AD0417F CRC64;
MLLLGAAGGG AYAWLRATSE PQRAGNVDLT GLGGRVQVTR DAWGVPHIRA QTDEDAVFAL
GFVHWQDRAW QMDFQRRVAQ GRLAEVLGEA ALPQDRFLRT WGFQRAAQSA LPALDARSRR
LIAAYTAGVN AAQGRGKKAL EFRILGYTPE AWQDVDTVSW SKLMAFDLGG NYDDEVMNAR
VARRLGAGGL DQVTAPYPAN GPTILSADEV GAQSAAPQTG ATSDAPRLPD TPSLPVETVA
ALRAHLRAAE ALGMQHVPGK GSNDWVIAGS RTATGKPILA DDPHLALTAP MLWYLADVQG
SELKAIGASI PGLPAIVIGR NARVAWGVTN MNPDVQDLYV EPEGARLTSR QEVIRVKGQA
DVTITVRESE HGPVISDNGG GGLNFADAGP RVALKWTALQ PGDTTMDAFL GLNYAQNWPD
FTRALSRYVG PSQNFVYADV DGNTGYYAPG RVPIREGWDG SLPVPGDGSR EWRGFIPFGE
LPHTFNPADG LVVTANNKVV PDGYPYLLGN TRNWAEPYRA RRITDLLTAT PKLSVADVQR
TQLDTRSLVW ADFRPILLAT KPGSDRARQA LGTLQGWDGN MTTGSVGALL FEAWLMQLQE
MASDELNDAT VMNSLSVLNQ LRGGGELCAQ GGQGDCAALL TRTLDAAITD LQARLGDDMT
GWTYGTLHQV ASNHRAFGKV SALAWLFNHH APTPGGTNTV NVARPEHGTY AQTHGASYRQ
IVDLSDPDRS LYIGSLGQAG SPLAPHATDQ MNRWIGGQYL PMSTKPADWG NTQTLTLHPA
GQ
//
