ID A0A1Y2DL73_9PEZI Unreviewed; 540 AA.
AC A0A1Y2DL73;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN ORFNames=BCR38DRAFT_350366 {ECO:0000313|EMBL:ORY59987.1};
OS Pseudomassariella vexata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY59987.1, ECO:0000313|Proteomes:UP000193689};
RN [1] {ECO:0000313|EMBL:ORY59987.1, ECO:0000313|Proteomes:UP000193689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY59987.1,
RC ECO:0000313|Proteomes:UP000193689};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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:ORY59987.1}.
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DR EMBL; MCFJ01000012; ORY59987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2DL73; -.
DR STRING; 1141098.A0A1Y2DL73; -.
DR InParanoid; A0A1Y2DL73; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000193689; 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 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:UP000193689}.
FT DOMAIN 82..528
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 137
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 540 AA; 59140 MW; 6A7A2793BBAD1B0F CRC64;
MGSQTSGNWK ELAQICVKIQ QDSIPKQWML SKDKLPSEET LNVSSVPYDA GTMSAEELEM
TAQDAGGLLK AYESGRWTVK QVITAFLKRG TVMQQMTNFA TEFLAESALQ KAEELDAQFK
ETGKLSGPLH GIPVSVKEHI GMDGHITHAG FVSKIGNVPK EDALSIQLLK KAGAVIHVRT
NQPQSLMHLD SNNNITGMTL NPLNLKLSPG GSSGGEGVSV GSKCSVIGVG TDIGGSVRAP
AAFNGCYGLR PTALRVPNLG NFGITAGQES IRGVVGPLGQ SVEDLELFMS AILGGKPWDV
ETMLVPIEWR KLAPNKEMTV GILYDDGIVK PHPPMVRALK IAAEKLNSAG IKVVNWEPFE
HQRGWDIVSA LYFPQGPSPY LDTFAETGEP VLPLTQHAFN FSSKEPLTIA ENWSLNYQKE
AYRREYHALM KERGVDFILC PAYPGAGVLQ GMAKYWNYTA IWNILDQPAS IFPSGVKVDK
DIDRPYEGYT PRNGHDEWEL KAYDPELMHG FPVCLQLAGK HFHDEEVLQA SKLIDAILKK
//
