ID A0A1M6ILA0_9PROT Unreviewed; 790 AA.
AC A0A1M6ILA0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SHJ35187.1};
GN ORFNames=SAMN02745194_02374 {ECO:0000313|EMBL:SHJ35187.1};
OS Roseomonas rosea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Roseomonas.
OX NCBI_TaxID=198092 {ECO:0000313|EMBL:SHJ35187.1, ECO:0000313|Proteomes:UP000184387};
RN [1] {ECO:0000313|EMBL:SHJ35187.1, ECO:0000313|Proteomes:UP000184387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14916 {ECO:0000313|EMBL:SHJ35187.1,
RC ECO:0000313|Proteomes:UP000184387};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQZF01000012; SHJ35187.1; -; Genomic_DNA.
DR RefSeq; WP_073135037.1; NZ_FQZF01000012.1.
DR AlphaFoldDB; A0A1M6ILA0; -.
DR STRING; 198092.SAMN02745194_02374; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000184387; 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:UP000184387};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT ACT_SITE 269
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 790 AA; 85095 MW; EB6E5AB3D1F7AF91 CRC64;
MASPPRRVRP VIRHQGRHPG RHLGRWLRRT LLILVALPLL LLAAAAGAIW WTLPGEAEAL
RLSGVSGPVE IGFDDRGIPR IRAASERDAA MALGVLHARD RMFQMEMTRR GGAGRLSEIA
GASTLRLDRF MRTLGLRQRA EADLAALPAE ARDMLQAYAD GVNAWARARG RFVAPEFIAL
GEPEPWRPAD SLLWGKVMGL WLSGNWRTET ERARLAGILS AERMEQLWPA DESLGRADLA
ALPQPARLAS LLKAVPRWGE DAPLPNSASN AWAVAPPRSV TGGALLASDP HLGLQAPVLW
YLARVELPGG RFLAGATAPG VPMIVIGRNE SLGWGFTTTH SDTQDVFVER LAGPDAYQTP
DGPRPFTTRE ERIAVRGRPE EVLRVRETRH GPVISDLDEE PPGEQVLAVA MASLAPADTQ
AAGLLALNRA RSVAEARAAA ALIASPAQNL MVADAAGGIA MFLTGRTPRR AAGDGTLPAP
GWDGSHDWTG WVPFEEMPHV VAPPGGVIAN ANNRVQPAGS NVFLGRDWFG DWRFRRIGDL
LRQRPRHAPG DFAAMQADAV SLLAREMLPL LLAPPRPEGM AGAARDLLPG WDGRMGPELP
QPLVFNAWMR ELGRLAMAAG GVPEGSWTAG PEFLALLTRP EGAAWCGADG CEAMSMRALE
AAVASLSPRF GPDPHRWRWG DAHRVRLEHP LLRFVPLLRD LIRIEAPTPG DGQTVNRGGM
GRDFTHIHGP GLRIVMDLSS PDGVLAAIAT GQSGNPFSRH WGDRTAGWAA GQAEALPAIA
PARARLRLDP
//