ID A0A1F8AGT8_9EURO Unreviewed; 522 AA.
AC A0A1F8AGT8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN ORFNames=ABOM_000716 {ECO:0000313|EMBL:OGM50924.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM50924.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM50924.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate +
CC NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001311};
CC -!- SIMILARITY: Belongs to the amidase family.
CC {ECO:0000256|ARBA:ARBA00009199}.
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:OGM50924.1}.
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DR EMBL; LYCR01000002; OGM50924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8AGT8; -.
DR STRING; 109264.A0A1F8AGT8; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR PANTHER; PTHR46072:SF5; GENERAL AMIDASE-C; 1.
DR Pfam; PF01425; Amidase; 2.
DR PIRSF; PIRSF001221; Amidase_fungi; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179}.
FT DOMAIN 80..160
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT DOMAIN 166..506
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 136
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 217
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 214..217
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
SQ SEQUENCE 522 AA; 56275 MW; B941262591E3361B CRC64;
MTILNWQQKA AAKQAEAAAK IPQEWRVPAD ILQVLENEQG VLTIPQRCGI LTPKELEITE
VADATTLRDR LAAREVTAVE VATAFCKRAA IAQQITSCLT ETMFPQALAR AKELDEYLLT
TGKPMGPLHG VPISLKETFN VQGVHSSLGL VSFLDRPEAC HNSALTMMTA DSENNVFGRV
LNPHRRNLTA GGSSGGEGAL VALRGSLLGI GTDIAGSIRI PALCCGTFGF KPSVGRVPYA
GQASAARPGM TGIAPVAGPL CHSARDAELL LRVVMEAPVD DLDDTVLGFP WTEPAPLATP
TLTIGVLPED PQAPLHPNMQ RTLKTAVERL AAAGHHIVDL SGQIQCIHEA SDISFRFFRI
DPDQTQVNHV SSSGEPYIKS LRYTYNLEGD DPEPTLRDLF DLNVARANVA AVMRRVYVEN
RLDVIIGPGN QSCAGPHDTY GVPVYTVLAN LVDYPACVIP FGKANEAADA EYVRDVAYIP
PYVPKEVENA PCHVQLIGRR LKDERLMQHA KIVESVLAGK SA
//
