ID A0A1H4G2W1_ALKAM Unreviewed; 795 AA.
AC A0A1H4G2W1;
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:SEB03929.1};
GN ORFNames=SAMN04488051_1176 {ECO:0000313|EMBL:SEB03929.1};
OS Alkalimonas amylolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alkalimonas.
OX NCBI_TaxID=152573 {ECO:0000313|EMBL:SEB03929.1, ECO:0000313|Proteomes:UP000198773};
RN [1] {ECO:0000313|EMBL:SEB03929.1, ECO:0000313|Proteomes:UP000198773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3430 {ECO:0000313|EMBL:SEB03929.1,
RC ECO:0000313|Proteomes:UP000198773};
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 -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit processed
CC from the same precursor. {ECO:0000256|ARBA:ARBA00038735}.
CC -!- SIMILARITY: Belongs to the peptidase S45 family.
CC {ECO:0000256|ARBA:ARBA00006586}.
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DR EMBL; FNRM01000017; SEB03929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4G2W1; -.
DR STRING; 152573.SAMN04488051_1176; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000198773; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000198773};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 249
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 795 AA; 88814 MW; 5A13CC125A3A30B5 CRC64;
MLVRYPLISR LFLFVILPLV IVVIWFGFSV LRSLPSYSSE YTVPFIDQPI EIHRDAYGVP
KIIAKTDQDL FFAMGFVQAQ DRLWQMEVNR RLGEGRLAEV LGASSVSTDI SMRTYGLALA
AEQAYISLAS ETKAVLQAYS DGVNAWVEQA DKLPPEFSLF SLQPEPWRPV DSVLVGKMLA
LRLAFGIQQE SDRQLAAAVL SPAQFANLYP GVVLETLPTE QIELISSQLN LGNAELSRDF
GIGITGVGSN AWVVSGKHTD TGRPILAGDP HLAVPIPSYW YQAELNGPVL KAKGVTVPGL
PVIVFGHNEF ISWNGTNFSA DAYDYVIEQI DPSRQNQYKT AQGWKSLQTR QETIHVRTAF
PGRLRPPARP IMITVTSTEN GPLIGYQNGD TSAMALKWTA LQPEDQTMTA LLQLNYASDW
HSFRAALSLM VAPTINFLYA DQLGNIGYAA AGHIPIRRNS TGILPTPQHK FAWTGMIPWE
EMPQQFNPAS GYIVNANQNN IPADYPYYVS YDWLDPARAN RIEQLLQHYI DSGNKLTLDS
MRKIQLDQLD MVAPRLIKRW CTDPEVEKKY TSLCSWDGNM QTDPAAAALY QLTLRHLTRT
LFSSTFATIN DRRLQQRWVG PRSFEDLPTR QQFKAALDQP ELWCEPKPVG CRAETLVALG
SATAELTRLQ GSNSKDWAWH NLAPRIYENF LFSQSNASRS LFERKVPGVG SYDTVNVGGY
RYDPLLGYQQ FFGASYRQVI VSEAHGFSYH AVNSTGQSGH PFSSHYADQL SAFTAGQLIP
PTDATRHLTL LRPHL
//
