ID A2QBK2_ASPNC Unreviewed; 540 AA.
AC A2QBK2;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN ORFNames=An02g00340 {ECO:0000313|EMBL:CAK96249.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK96249.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK96249.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM269996; CAK96249.1; -; Genomic_DNA.
DR RefSeq; XP_001399172.1; XM_001399135.1.
DR AlphaFoldDB; A2QBK2; -.
DR EnsemblFungi; CAK96249; CAK96249; An02g00340.
DR GeneID; 4979617; -.
DR KEGG; ang:An02g00340; -.
DR VEuPathDB; FungiDB:An02g00340; -.
DR HOGENOM; CLU_009600_9_2_1; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000006706; Chromosome 4R.
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, ECO:0000313|EMBL:CAK96249.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 82..528
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 138
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 238
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 235..238
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
SQ SEQUENCE 540 AA; 58939 MW; 5C7545A883CE870F CRC64;
MAVEQWETIV QKKQADAAAK IPQAWRLPAE FTAHVSETAS TNVLDVPRKC GLLSAKQLEI
TENYDATALL EQIHSGKLTA VEVAEAFCLR AAIAQQVTRC LTETFFDLAL ERAKELDEYF
QSTGKVRGPL HGLPISLKDC FNVAGVPNTI GFTAFIAHGP VKNNSSVVQI LLDLGAVLYV
KTNIPQTMMA ADSHNYVFGR TLNPNRTKLS AGGSSGGEGA LIAMRGSILG VGTDIAGSIR
IPGIFDGTYA LRPSIHRIPY GGQTGSGRKG LAGIRPCAGP LATSVRDLGL FMKTVVDIDP
WQYDSSTIFS TWRTAPPKET LRLGFILEDP HFPVHPPILN TLTRAVDALK AAGHEVINLT
TPSIRDALLL GFRTFAMDPA RTAFSHITKS GEPRIPALRT TDLPNADLPF EWAPHTLESL
YDLNVQRETL CEQFRQLIVQ NKIDAIIMPG YQGTAVAHDQ VGWVPYTVLA NVLDYPATII
PYRKADKADD AKYVRDVTYR PPYVADDVEG APCCVQLMGR TMHEEELLRD TAIVARVLGK
//
