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}.
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; 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
//