ID A0A239KGV5_9SPHN Unreviewed; 732 AA.
AC A0A239KGV5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Acyl-homoserine-lactone acylase {ECO:0000313|EMBL:SNT17401.1};
GN ORFNames=SAMN06295955_11447 {ECO:0000313|EMBL:SNT17401.1};
OS Sphingopyxis indica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=436663 {ECO:0000313|EMBL:SNT17401.1, ECO:0000313|Proteomes:UP000198339};
RN [1] {ECO:0000313|EMBL:SNT17401.1, ECO:0000313|Proteomes:UP000198339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS15 {ECO:0000313|EMBL:SNT17401.1,
RC ECO:0000313|Proteomes:UP000198339};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FZPA01000014; SNT17401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239KGV5; -.
DR Proteomes; UP000198339; 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; cd01936; Ntn_CA; 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: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; 3.
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:UP000198339};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT ACT_SITE 230
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 732 AA; 80404 MW; 6A34B637EAB4F463 CRC64;
MRARRTIIMQ RVGKRMRKFF LGLLLLLAAV AIGLAIWEPL TAEAPAAPAY KVGDVRIARD
KFGVPHIFGK TDADVAYGVA FAHAEDDFST LQEVLAMTRG RAGAMLGPDG AKIDYVAALL
GVRDTTARDW PRLPADVRAL FTAYAAGLNH YAEKHPGEVR MRGLFPVTGE DVVAGFVLRS
PFFFGLDSVL GKLAAGEPLG REGGPAIDVT GKVVPRADTP LGSDPGESGS NGIAVAPSRM
ADGTTRLVSN SHQPWTGGVA WYELVVHSQQ GWDFAGANFP GSPYPFLGHN KYLGWTNTVN
RPDLIDVYKL TLDESGKNYR FDGRWLPLEK KRIWLKVKFG PFVLPVPRTV YRSVHGPVIE
NDQGAFAIRY AGQDQANMVT QYYRLNKAKS FAEWRAAMAA QGVPATNFIY ADAKGNIGLF
YNAMFPDRPR GFDWRTILPG DTSADLWTKT LPFDRVPALV NPASGYVINA NNTPWVAAGP
GDELDPAAFS PLLGIEDDMT NRAARLIQLF EASGKIDEAR LRQIKYDTAY AKTGYAKAWI
DKLLALDTKG DPALAEAQKL LREWDWNLDG KGHGDALALM VLRPAGSAHY QRRADPDPRE
VLSEVAAHLR QYFGSLDPKL GTVLRLRHGE GAHRVDLPLD GGNDTVRAST LWDAEPDGRL
KVRHGDSFIM FVTWDKAGRV HSQSIQPFGA ATTRPDSPHY NDQAPLFVRH QLKPVLFDPA
ALRASGARFY RP
//
