ID A5PCH9_9SPHN Unreviewed; 731 AA.
AC A5PCH9;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 03-MAY-2023, entry version 56.
DE SubName: Full=Penicillin amidase family protein {ECO:0000313|EMBL:EDL48749.1};
GN ORFNames=ED21_31129 {ECO:0000313|EMBL:EDL48749.1};
OS Erythrobacter sp. SD-21.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=161528 {ECO:0000313|EMBL:EDL48749.1, ECO:0000313|Proteomes:UP000005498};
RN [1] {ECO:0000313|EMBL:EDL48749.1, ECO:0000313|Proteomes:UP000005498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD-21 {ECO:0000313|EMBL:EDL48749.1,
RC ECO:0000313|Proteomes:UP000005498};
RA Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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:EDL48749.1}.
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DR EMBL; ABCG01000005; EDL48749.1; -; Genomic_DNA.
DR RefSeq; WP_006833856.1; NZ_ABCG01000005.1.
DR AlphaFoldDB; A5PCH9; -.
DR STRING; 161528.ED21_31129; -.
DR MEROPS; S45.002; -.
DR eggNOG; COG2366; Bacteria.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000005498; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000005498};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT ACT_SITE 231
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 305
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"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 731 AA; 81715 MW; 1993DA3CBA6AA270 CRC64;
MKKWSLRIGA AVLVILLAAF IGLATWEPFW AKREAIAAQQ ATYTAEIIRD EFGVPHIYGE
RDRDVAYGVA IAHSEDDFST LQDVIAMARG RYGAIAGEDG AAIDYVFHLL DARGTAEQHY
PELPEDTRAL FEAYATGLND FAADNPDEVK LGNLFPVTGT DVAAGFALRQ PFFFGLNGVI
EPLVKGEDLR REYGPDIPGF PREGTPPDEQ PVHESDVAYS PFGRDGAMSG SNAFAVAPEK
SGGPTILVSN SHQPWRGGVA WYELVVESEE GWHYAGANFP GSPFPFLGHN ETLGWTNTVN
TPDMVDVYEL EMDESGRRYR FGGEWRDLEV ESVTLPVRFG PVTLPVWRDV YRSVHGPVIR
NERGTFAFRY GGIDNLGQLD AYYRLNKVET LEEWQAILAR MDIPSTNFIY GDREGNIAYV
YNAALPDRPQ GPNWRGVLDG SDPALLWDGP VEYEELPRYV NPASGWLYNA NNTPFTAAGA
ESDLVASQFA PELGVELKQT NRSRMAWKLL SEADRLDSDT LRRIKYDTSY AREGYIADLW
DALAALDLSD RPDLAPARNL LLAWDFKADN IGRGDSLALL MIREFMSCRY QNKPCPEVLG
ELEKAVDHLE TYFGRIDPPM GELLRLRQGS VDLPLDGGSD TLRASTLWDV EEDGRLAVRH
GDSFIQWVEW LPGERVTSRS IQPYGAATTR PNSPHFADQA TLFVQHRMKP VHFWREDVLA
NAVTRKTVTH R
//
