ID A0A1V2H4G8_9PROT Unreviewed; 791 AA.
AC A0A1V2H4G8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Penicillin acylase {ECO:0000313|EMBL:ONG55008.1};
GN ORFNames=BKE38_09650 {ECO:0000313|EMBL:ONG55008.1};
OS Pseudoroseomonas deserti.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Pseudoroseomonas.
OX NCBI_TaxID=1817963 {ECO:0000313|EMBL:ONG55008.1, ECO:0000313|Proteomes:UP000188879};
RN [1] {ECO:0000313|EMBL:ONG55008.1, ECO:0000313|Proteomes:UP000188879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3 {ECO:0000313|EMBL:ONG55008.1,
RC ECO:0000313|Proteomes:UP000188879};
RA Subhash Y., Lee S.;
RT "Draft Genome sequence of Roseomonas sp. strain M3.";
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}.
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:ONG55008.1}.
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DR EMBL; MLCO01000077; ONG55008.1; -; Genomic_DNA.
DR RefSeq; WP_076957164.1; NZ_MLCO01000077.1.
DR AlphaFoldDB; A0A1V2H4G8; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000188879; 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:UP000188879};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT ACT_SITE 256
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 331
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 791 AA; 86591 MW; 7D63D335866CAAFC CRC64;
MNDTVAPPAS PTLPGETIRL RGLQAPASIH VDRWGIPHLR AENEADLFFL QGFNAARDRL
WQIDLWRKRG LGLLAADFGP GFLAQDRASR LFLYRGDMEA EFSAYAPDAR QICEAFVAGI
NAFVDLVEAE PARLPAEFRA LGTRPSRWAA EDVVRIRSHS LTRNALSEVL RAIVLSKADL
ATDLLRKHLE PMVEPVRPEG LDLSTLGTEV LTQFKLATAA VTFSAERLAA PLDDWRRWTA
VTDLGDVVMG AEMEGSNNWA IHGSRSESGR PILASDPHRA HAAPSLRYIV HLDSPGFNAI
GAGEPAVPGI SIGHNGTSAF ALTIHGADQE DVYVYETAEG DRNSYRHGDA FSDMDVVRDN
FAVKGHPDQT LMLRFTQHGP VIAEDVANRR AVAIRTVWSM PGSAPYLASL ASMRATTLEE
FRTAIRRWGT PSVNKVYADT SGTIAWTPAG FAPQRPNWDG LLPVPGDGRY EWSGLLDPAE
HPWRVDPLEG FVHSANEQNL PADWNHAEKT YGYEWVEASR ATRIRESLTR GPLLTLADCT
ALQTDVLSIP ARRLCALLLT LPRGSAPELW AAQTLLEDWD FRLAADSAAA GLFEVFLTKH
LKPRLLAALV PDATLRPLLL PQDMESLLLV LENPDARLPA AARDALLADC LMAAFHDCES
RMGSCPSGWS WGKLHHGYFA HALQGLTAET ATLDVGPFPV GGSAQTPMHT GYRPGDFRCT
FGASVRLVMD VGEWDNSLCI NAPGQSGDPA SPHYADLAPH WAQGEYVPLL YSREAVDRME
MQRIALVPVA D
//