ID B8MWW4_ASPFN Unreviewed; 560 AA.
AC B8MWW4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN ORFNames=AFLA_075510 {ECO:0000313|EMBL:EED56856.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED56856.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED56856.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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}.
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DR EMBL; EQ963472; EED56856.1; -; Genomic_DNA.
DR RefSeq; XP_002372468.1; XM_002372427.1.
DR AlphaFoldDB; B8MWW4; -.
DR STRING; 332952.B8MWW4; -.
DR EnsemblFungi; EED56856; EED56856; AFLA_075510.
DR VEuPathDB; FungiDB:AFLA_003104; -.
DR eggNOG; KOG1212; Eukaryota.
DR HOGENOM; CLU_009600_9_2_1; -.
DR OMA; VIGPCGR; -.
DR Proteomes; UP000001875; 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; 1.
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}.
FT DOMAIN 80..544
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 212
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 236
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 233..236
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
SQ SEQUENCE 560 AA; 60753 MW; D8975C33C0D062A2 CRC64;
MTIPDWQQKA AAKQAEAAAK IPKEWRVSAS ILENLDNEQE VLTIPQRCGI LSPKELEITE
TVDATTLRDK LAARELTAVE VTTAFCKRAA IAQQITSCLT ETMFPQALAR AKELDEYLQT
TGKPMGPLHG VPISLKETFN VQGVHSSLGL VSFLDRPEAS HNSALVEILL AAGAVLYVKT
NVPQTMMTAD SENNVFGRVL NPHRRNITAG GSSGGEGALI ALRGSLLGIG TDIAGSIRIP
ALCCGTFGFK PSVGRVPYAG QASAARPGMA GIAPVAGPLC YSARDAELLL RVVMEAPVDD
LDDNVLGFPW IEPAPLAAPT LTIGVLPEDP QVPLHPNMQR TLKTAVERLA AAGHRIVDLS
GQIQCIKEAS DISFRFFRID PDQTQVKYVS SSGEPFIKSL RYTYNLKGDD PEPTLRDLFD
LNVERAKVAA IMRRLYVENK LDVIIGPGNQ SCAGPHDTYG IPVYTVLANL VDYPACVIPF
GKANEVADVE YVRDVAYIPP CKNFNCSYEP LRNPILTIID CPKEVENAPC HVQLIGRRLK
DERLMQHAKI VESVLASKST
//
