ID A0A1I2E7G8_9RHOB Unreviewed; 773 AA.
AC A0A1I2E7G8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SFE88653.1};
GN ORFNames=SAMN04488523_111143 {ECO:0000313|EMBL:SFE88653.1};
OS Sulfitobacter brevis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=74348 {ECO:0000313|EMBL:SFE88653.1, ECO:0000313|Proteomes:UP000198977};
RN [1] {ECO:0000313|EMBL:SFE88653.1, ECO:0000313|Proteomes:UP000198977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11443 {ECO:0000313|EMBL:SFE88653.1,
RC ECO:0000313|Proteomes:UP000198977};
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; FOMW01000011; SFE88653.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2E7G8; -.
DR STRING; 74348.SAMN04488523_111143; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000198977; 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:UP000198977};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT ACT_SITE 243
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 773 AA; 83598 MW; A419D64526CC7866 CRC64;
MTAFTLKGLE APASISVDTW GMAHIRAETT RDGFFVQGFN AARDRLWQID LWRKRGLGLL
AADFGPGYLM QDRAARLFLY RGDMAPEWAA YGDDAEMICT AFAAGINAGI DQVLSGALPM
PPEFTELGTK PARWSAEDVV RIRTHCLSRN AGSEMARAKV LSLADPDVDL LRQPLSPAVP
KTEWQSTSTT ALPDGALSVY DLATAPVTFS PQRLAATLDE APLWSGVDAR KTVHRAEPPM
EGSNNWIVAP ALTTSGRAIM ASDPHRAHAA PSLRYMTHIK TPDLDLIGAG EPSSPGIMAG
HNGQAAFSLT IFCADQEDLF VLETTPDGSA YRDGDSFAPL TRTEEVFAVK GEADQTLPLL
FSHHGPVIFE DKARQMAVAL RTVFTDAGTA PYMCSLKTMR STTVAGFQKA AETWGAPSVN
LIYADVAGDV CWQAAAYVPR RNGWRGLTPV AGDGQFKWDG YLTAADLPST VNPDCGFVHS
ANEMNLPDSW DHTQFPVGFE WFEDGRADRV ADVIAAKGAS DIAANCALQT DTHSSLALRL
VTLLPDSIPV PARALLRQWD GRADAGSAAA LLFEVWLSSH LRPRLLELVA PDLSLRKYLQ
PGNIPTVVRL LEGAHPSLAA RAGLAEDAAR DAFLAQTLDQ AWQDISSRFG ENPDDWRWGD
LHKGWFDHAL TPVKPGFDVG PLAKSGNSTT VMLAHYDASD YRVTVGASVR MVVDVGAWDN
SVWINAPGQS GLPQDPHYDD LAPVWAEGEY VPLLYSDAAV AEATQTRIEL TPA
//