ID A0A1H8KJ58_9FLAO Unreviewed; 733 AA.
AC A0A1H8KJ58;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acyl-homoserine lactone (AHL) acylase PvdQ {ECO:0000313|EMBL:SEN92942.1};
GN ORFNames=SAMN04487942_1197 {ECO:0000313|EMBL:SEN92942.1};
OS Flavobacterium sinopsychrotolerans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=604089 {ECO:0000313|EMBL:SEN92942.1, ECO:0000313|Proteomes:UP000198657};
RN [1] {ECO:0000313|EMBL:SEN92942.1, ECO:0000313|Proteomes:UP000198657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8704 {ECO:0000313|EMBL:SEN92942.1,
RC ECO:0000313|Proteomes:UP000198657};
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; FODN01000002; SEN92942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8KJ58; -.
DR STRING; 604089.SAMN04487942_1197; -.
DR Proteomes; UP000198657; 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; 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; 2.
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 Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT ACT_SITE 202
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 733 AA; 83610 MW; 75E04EC6EB1F42C4 CRC64;
MKHFKYHLPL IVLVFCFGFP MFSQKTSNQE IERLKKLSQQ VTIIRDNWGI AHVYGKTDGD
AVFGMLYAQC EDDFKRVEMN YIEKLGRLSE IKGQSVLYND LEIKLLMDTE EAKADYKKAA
PWLKKLLNSY ADGINFYLHN HPEVKPALLT HFEPWFPLLW TDGSIGAIST ANLTTGELKA
FYSGNTDKVA YIEREKDVQT GSNGFAIAPS KTASGNSILY INPHTTFYFR PEIQMSSEEG
LNAYGAVTWG QFFIYQGFNE NCGWMHTSSN VDVADMYAEK IVTKNNNLFY EYDNKLVPVI
EKKITIKYLE NGKLIPKTFN TYYTNHGPIM AKRDGKWISL KSNNRSMKSL EQSWIRTKSK
SFADYKSAMD LKANTSNNTV YADKEGNIAY WHGNFVPIRD KKLNWSKVMD GTTPTTQWKG
LHEVSETVHS YNPINGWLQN CNSTPYTVAG ENSPKEENYV PYMAPDGESF RGLNAVRLLS
KGDKYTLDKV IADGYDTKLT AFEFLIPALI SSFEKNISTE DPLYTELLEP ITLLKNWNYY
AKENSVATTL AVEWAYKLDP IIQKVYTNEG ELDQIENTSN FAKNAFPDQL IPQLQMVVND
LKIKFGTWQI PWGEINRFQR TSGDINLIYN DALESLPIGY GPALWGSLPA YKSNYQKDTK
KRYGTNGNSF VCAVEFGPKI KAKSILAGGN SGDPKSKHFY DQAEMYRKGQ FKDVLFYKDD
VQKNAEKTYH PGE
//
