ID   A0A1H7XAL8_9BACT        Unreviewed;       810 AA.
AC   A0A1H7XAL8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SEM30860.1};
GN   ORFNames=SAMN04488505_10414 {ECO:0000313|EMBL:SEM30860.1};
OS   Chitinophaga rupis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=573321 {ECO:0000313|EMBL:SEM30860.1, ECO:0000313|Proteomes:UP000198984};
RN   [1] {ECO:0000313|EMBL:SEM30860.1, ECO:0000313|Proteomes:UP000198984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21039 {ECO:0000313|EMBL:SEM30860.1,
RC   ECO:0000313|Proteomes:UP000198984};
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; FOBB01000004; SEM30860.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7XAL8; -.
DR   STRING; 573321.SAMN04488505_10414; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000198984; 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; 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:UP000198984};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        278
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         350
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         353
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   810 AA;  91785 MW;  8FE6207FF148683C CRC64;
     MRFIPFLIAA VITLALIGAL NRKWGSIPPL GKFLSPQEGF WQNAEAISKD YNEELALPGL
     KGKVEVWLDD RMVPHIFAEQ EADAYYAEGY LHARDRLWQM ELQTMAAQGR LSEILGPKLL
     QYDRRQRRLG MGYAAELSAA AMLKDSTTKM VVEAYSAGIN AYISSLSYSD LAVEYKLLDY
     RPEPWSALKC AALLKYMSYD LAGGVNDLEY TNARRLFSPS DFNNMYPDRN DSIDPVIPKG
     TAFDKPVKNA VMPADSALQE VAAMLHFKQD KPDPDNGSNN WAVSGSKTRS GAPILCNDPH
     LGLSLPSLWY EVQIKTPGMN VYGASLPGAP GVIIGFNDNI AWGVTNGSED VMDYYAVQFR
     NGRQQYLFNG QYRDAVPRVE EIKIRGQQSY YDTVAYTVWG PVMFDNTFHD DIPGQPFLAL
     RWKAHDPSNE LLTFNRLNHA RNYDDYVAAL EHYTCPAQNF VFASKAGDIA LWHNGEFPLR
     WKDQGKWIMP GSDSTFAWQG YIPHGEVPHI KNPARGFVSS ANQQPTDSSY PYYYFGYYDL
     YRGKRINERL SAMSQITTQD MMQLQNDNAN LFARAAIPLL TRHLPEADLK PAQQPYYQLL
     KVWDQQNSPG SKGATIFYML WEGLKHRIWD DELMNRADSL ALDYPQDNAS LLWLIRDSSM
     RFVDDVHTPQ KETLTDLVLQ TFAQVTDSAQ KLDQRQELEW GRFRGTDIRH LTRSLPAFSR
     MHLYTGGGTH VVNATKANHG PSWRMVVQLG ATTEAYGIYP GGQSGNPGSP YYDNAVSDWV
     QGKYYLLHIF DQKQRDDAGI KFRMVMQPKS
//