ID A0A1B8ES29_9PEZI Unreviewed; 536 AA.
AC A0A1B8ES29;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN ORFNames=VF21_06286 {ECO:0000313|EMBL:OBT74176.1};
OS Pseudogymnoascus sp. 05NY08.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622149 {ECO:0000313|EMBL:OBT74176.1, ECO:0000313|Proteomes:UP000092096};
RN [1] {ECO:0000313|EMBL:OBT74176.1, ECO:0000313|Proteomes:UP000092096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05NY08 {ECO:0000313|EMBL:OBT74176.1,
RC ECO:0000313|Proteomes:UP000092096};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05NY08 {ECO:0000313|Proteomes:UP000092096};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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; KV458849; OBT74176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8ES29; -.
DR STRING; 1622149.A0A1B8ES29; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000092096; 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:SF11; AMIDASE-RELATED; 1.
DR PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 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:UP000092096}.
FT DOMAIN 82..512
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 124
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 199
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 223
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
SQ SEQUENCE 536 AA; 58810 MW; 9E3DF207070C3CA4 CRC64;
MESNKESWES IAKAKRQSLA AAIPKEWIIP AEILPPPIQA DVTTFPSKSG WFTKRELDIL
STDAAKILKC LSTGAWASEE VTRTNCLSEI FFDEAIARAK ECDAYLQKYG KIKGPFHGLP
ISIKDNFNII GKDSTIGMTS LVNKPATYNS TLIDIILDAG AVLYVKTNVP TAVMLPETVN
NVFGRTLNPL NRNLTPGGSS GGESALLAFG GSRIGVGSDI GGSLRIPAAC TGTFTLRPSA
GRFPHCRARS GLTGQEAVNS VNGPMAKTLE EIVLYSKIII DQQPWFLDPK CLPIPWRSIE
PKKHLKLAVF WHDGVVTPTP PVARALRETV KRLRAGGHEI VEWDPVEHKT ANSLLRRMFI
ADGAKSIRGL LAPTNEPFRP EMPSYEGSVE LGVHEMWQIQ AERSDLQKRY LDRWNALGVD
GLICPTSPYS SVEHGKFTYG GYTGVYNLLD YSAVSFPCGV TVDKNVDAAY SKHHPLSEID
AQVQRDYDAT IVNGMPVSLQ LVARRLEEEM VLMMTDVVLQ SLQSSGISIS RTRSNL
//
