ID A0A0J1HEN0_9GAMM Unreviewed; 820 AA.
AC A0A0J1HEN0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Penicillin amidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ABT57_09285 {ECO:0000313|EMBL:KLV10061.1};
OS Photobacterium ganghwense.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=320778 {ECO:0000313|EMBL:KLV10061.1, ECO:0000313|Proteomes:UP000035909};
RN [1] {ECO:0000313|EMBL:KLV10061.1, ECO:0000313|Proteomes:UP000035909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22954 {ECO:0000313|EMBL:KLV10061.1,
RC ECO:0000313|Proteomes:UP000035909};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLV10061.1}.
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DR EMBL; LDOU01000007; KLV10061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1HEN0; -.
DR STRING; 320778.ABT57_09285; -.
DR PATRIC; fig|320778.3.peg.2020; -.
DR Proteomes; UP000035909; 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 Gene3D; 1.10.1400.10; -; 1.
DR Gene3D; 1.10.287.150; -; 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:SF3; ACYL-HOMOSERINE LACTONE ACYLASE PVDQ; 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:UP000035909};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT ACT_SITE 271
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 522
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 820 AA; 91700 MW; 8CA57818857EB5A2 CRC64;
MPEASLAETR QAAQEDITIL RDNYGTPHIY ADNTYGLFYG FGYAIAQDRL YQLEMAKRSA
QGKVAEVLGK EYLPLDIKVR EHYNPDAIRQ ALNALPPEDA EIFQGYADGL NAWIRHIEQS
PDTLMPKQFL DGHFAPTQWQ PFDVVMVFVG SMINRFGDYN TELENQQLLQ ALQQQHGKTK
GRALFDALLP YQSQQAVDTI PDGEWTAQAR QKIRNERVAA LRQTNSEGAV IAKTSAAPTT
QALFTDETTL AARTGLEGTL GWRGFKEAPF SNILVLGKAK TAGANAVLIN GPQFGFYRPA
YTYSVGLHGA GYDVVGNSPA GYPLVQFGHN QHISWGSTWG AGDNVDLFRL TLNPDNPEEY
LYKGRYIAFD KQHQTVKVKG EADRIITVYR SVHGPVINYD PQNQVAFAKQ RGWAGKELST
LLAWNKVAQA SNHQEWQQQV AQSAINVNWY YADQQGNIAY ALGGHYPIRH PGVDGRLPTN
GDGSADWLGL YPFSTNPQVL NPGSGYIANW NNRPAKGFPN PDQWWYSWNT VDRNLEITRR
VDAANLLTAQ DAWQLMMDAS LSDPNARHFV PQLVTLARHS QDPALQQAAE VLASWDYRNT
DDNGDGRYDH PASTLFRTWL SEALTLTYTP LLPDPQRGWF TNPGYGNKER VLTNSYNIQT
GTKALAAIWS NPTYLTTQKT DSLKLNALRT AIDHVTARYG TNSNSWHDEV DVLRFSHKNY
IGVPQAGQDE VTDTPIALNR GTENNMTVFG RDKIEAFEVA APGQSGFISP NGERSAHYND
QYEDFVQFRL KPVYSSREAL EQTSPDKTVL TVSLPDPQRI
//