ID A1CLX5_ASPCL Unreviewed; 536 AA.
AC A1CLX5;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN ORFNames=ACLA_078530 {ECO:0000313|EMBL:EAW09104.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW09104.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW09104.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027057; EAW09104.1; -; Genomic_DNA.
DR RefSeq; XP_001270530.1; XM_001270529.1.
DR AlphaFoldDB; A1CLX5; -.
DR STRING; 344612.A1CLX5; -.
DR EnsemblFungi; EAW09104; EAW09104; ACLA_078530.
DR GeneID; 4702556; -.
DR KEGG; act:ACLA_078530; -.
DR VEuPathDB; FungiDB:ACLA_078530; -.
DR eggNOG; KOG1212; Eukaryota.
DR HOGENOM; CLU_009600_9_2_1; -.
DR OMA; VIGPCGR; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000006701; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 80..523
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 536 AA; 57565 MW; 223BCC1EB6239667 CRC64;
MAILDWQQKA QAKQAEAADK IPSEWRLSAE LLKTTANDSN ILDIPTKSGI LSAHELDITG
NHDATALLQK LAARELTSVE VTTAFSKRAA IAQQLTSCLT ETFFDRALAR AKELDDHLAA
TGKPVGPLHG LPISLKETFS VQGIPTSLGY VSFLDRENPS TNSALVDILL AAGAVLYVKT
NVPQTMMTAD SHNNVFGRVL NPHRRNLTAG GSSGGEGALI AFRGSVLGVG TDIAGSIRIP
ALCCGTVGFK PSVGRVPYAG QTTGARGGMV GIGPCAGPLS HSLRDAELLL RTVFNSQPEN
LDDNVVGFPW VDAPSQPILT IGVMAEDPKF PVHPPMQRAL ALAVKKLEAA GHRIVDLSGK
LPSIAESCEL SFRYFNLDSD RTSLSHISAS GEPPIPSLRF TFDLDSKMPE LTLRDVFDMN
VQRAQITAQA RQAFLDNKLD VIIGPGYQSC AVPHDTFGAA PYTVFGNLID YPSCVLPFSK
AEQAADTEFI RDVTYIPPYL PKEVEGAPCH VQITGRRLKD EALMEHAKII EAVLLK
//
