ID   A0A1E3HEJ8_9TREE        Unreviewed;       418 AA.
AC   A0A1E3HEJ8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE            EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN   ORFNames=L202_06930 {ECO:0000313|EMBL:ODN74565.1};
OS   Cryptococcus amylolentus CBS 6039.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus.
OX   NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN74565.1, ECO:0000313|Proteomes:UP000094065};
RN   [1] {ECO:0000313|EMBL:ODN74565.1, ECO:0000313|Proteomes:UP000094065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN74565.1,
RC   ECO:0000313|Proteomes:UP000094065};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:ODN74565.1}.
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DR   EMBL; AWGJ01000011; ODN74565.1; -; Genomic_DNA.
DR   RefSeq; XP_018990346.1; XM_019141539.1.
DR   AlphaFoldDB; A0A1E3HEJ8; -.
DR   GeneID; 30158239; -.
DR   OrthoDB; 731186at2759; -.
DR   Proteomes; UP000094065; 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:SF4; AMIDASE C550.07-RELATED; 1.
DR   PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR   Pfam; PF01425; Amidase; 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:UP000094065}.
FT   DOMAIN          74..404
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
SQ   SEQUENCE   418 AA;  44893 MW;  105B1D28E2963843 CRC64;
     MADAWQSKAA QYRQNLQESI PPEWRISVTP SCYPVSEYLS QSSLFTHTEQ SILRLDATGL
     RDAIAAREFS ACSVTVAYAK AGAVAHQTTN CLFDFFPEEA IQRAKWLDEE MEKGGPVGAL
     HGVPISVKSS FGIKGHRMTR GFLSDVDSAP AEEDATIISI LRNAGAVFIL TTALPQSIMH
     LETDSFLGPC LNPHNPKLTP GGSSGGESAI IAAGCSVLGI GSDIGGSIRA PAGAAGIFGF
     KPTAIRLPKF GCTSMMPGQE AIPGAFGPMG KSPRDMELFV HTVLQAETWK TDPTQAGMPW
     VPGRVNWVGG DKLRVGVMWD DGVVVPQPPI QRALKTAADS LKKAGYEVVD FEPFKAAESW
     ELVSSLYFTD GGARINKCAA ESGEPVLPLT KWIMSQNSRE RTMEELHEVS SFMSTLLS
//