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Database: UniProt
Entry: A3I1W6_9BACT
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ID   A3I1W6_9BACT            Unreviewed;       804 AA.
AC   A3I1W6;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Putative penicillin G acylase {ECO:0000313|EMBL:EAZ79782.1};
GN   ORFNames=ALPR1_09158 {ECO:0000313|EMBL:EAZ79782.1};
OS   Algoriphagus machipongonensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=388413 {ECO:0000313|EMBL:EAZ79782.1, ECO:0000313|Proteomes:UP000003919};
RN   [1] {ECO:0000313|EMBL:EAZ79782.1, ECO:0000313|Proteomes:UP000003919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR1 {ECO:0000313|EMBL:EAZ79782.1,
RC   ECO:0000313|Proteomes:UP000003919};
RX   PubMed=21183675; DOI=10.1128/JB.01421-10;
RA   Alegado R.A., Ferriera S., Nusbaum C., Young S.K., Zeng Q., Imamovic A.,
RA   Fairclough S.R., King N.;
RT   "Complete genome sequence of Algoriphagus sp. PR1, bacterial prey of a
RT   colony-forming choanoflagellate.";
RL   J. Bacteriol. 193:1485-1486(2011).
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:EAZ79782.1}.
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DR   EMBL; AAXU02000001; EAZ79782.1; -; Genomic_DNA.
DR   RefSeq; WP_008200009.1; NZ_CM001023.1.
DR   AlphaFoldDB; A3I1W6; -.
DR   STRING; 388413.ALPR1_09158; -.
DR   MEROPS; S45.003; -.
DR   eggNOG; COG2366; Bacteria.
DR   HOGENOM; CLU_011790_0_1_10; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000003919; 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:UP000003919};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        277
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         349
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         352
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   804 AA;  92243 MW;  ED780911A792AA6E CRC64;
     MKYISFLLAL GITITLAIYV SKPIGPVPPI ATLIDPNHGF WQNMISEDDL AETEVLLEGL
     NSPVQIVYDK NLIPHIFAQN EEDLYKAQGY VTAKHRLWQM EFQTRAAAGR LSEIVGDVAL
     ELDRMTRRKG LGYGAELGMD FLKESDPETL RYLEAYASGV NQYINSIGPG QLPVEYKILN
     YRPEEWTPYK SLLLLKYMSD MLVGDRDLEY SNLRKILGEQ MLNKLYPDYP KDADPVIESD
     KVWEFEPLEI QKPDSLEYPD DLLSMKPLEQ PLPGTGSNNW AVAPSKTKNG HPILANDPHL
     SLNLPSLWYA IQLTTPDYSV KGASLPGALG VISGFNENIA WGVTNATKDA RDWYKITFQD
     EQRKAYKYGD QWRPTNFRIE EIKVKDQDAF LDTVVYTHYG PVVYDKSFRS ERQDVNFALK
     WTVHMGSNEQ KTFLLLNKAT NHEDYNVALD NFTAPAQNFV FASKNGDIAM RIQGKFALKW
     PEQGKFFMDG ADPRMEWQKF IPNEQNPSTL NPNRGFVASA NQHPVASSYP YYVFDNSYEH
     YRNRRINGKL REMEDITVED MKKLQFDDFY FQASEALPTM LNLLGGDYSK EGNTEKYIKQ
     LKEWDYYADP NQKAPTLYYV WWGKLYNQIW QAWDDFGVSV VKPNSYQTIQ LLKNEPNDSI
     FDLEKTQEIE NAKSHVLKSF EMMVKEISDW EQNEGDYAWA NFKQTSIQHL VPQFKSFSET
     NVYTGGGAGI VNATSERHGA SWRMVVELGD KPTAFGIYPG GQSGNPGSKY YKNFIPVWAE
     GNYLDFNLRS QKDTTNLLYQ TTLK
//
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