ID A0A1E4TJ87_9ASCO Unreviewed; 544 AA.
AC A0A1E4TJ87;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN ORFNames=CANCADRAFT_30132 {ECO:0000313|EMBL:ODV91806.1};
OS Tortispora caseinolytica NRRL Y-17796.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trigonopsidaceae; Tortispora.
OX NCBI_TaxID=767744 {ECO:0000313|EMBL:ODV91806.1, ECO:0000313|Proteomes:UP000095023};
RN [1] {ECO:0000313|Proteomes:UP000095023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17796 {ECO:0000313|Proteomes:UP000095023};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Jeffries T.W., Grigoriev I.V.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (FEB-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}.
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DR EMBL; KV453841; ODV91806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4TJ87; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000095023; 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:UP000095023}.
FT DOMAIN 85..531
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 240
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 237..240
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
SQ SEQUENCE 544 AA; 60317 MW; 774D0061C353813F CRC64;
MQTTEDPVKY EQWKSEIERV RKIRDDSIIK EYLIPEDKLP PADQLNMMNV PRESGIMTEK
ELTITETPVY ILAGEIAEGK YTAVETLTAF LKRATMAQQL LNCVTEFLAD EAMKLAESLD
KTFKETGKTV GPLHGIPLSI KEHLWVAGKE ANAGFVGFIG RVVDEDNLQL SILKKAGVVP
FARTNEPQSL MHADSYNNIF GMTWNPHNRL LTAGGSSGGE GSLVGFYGSS FGIGSDIAGS
IRNPAGFNGC YGYRPTAQRI TVKGRSGAGA GQITLLPSIG PFTQSADDLE LYMKTVTDGK
PWEVDCTIPI MPWRKVETPK SLTIGVMKED GIVYPLKPVF RALDHAIKKL EKAGHKVVTW
DPLNSKEIYE MALKSFFADG GTAQKKALEI SGEPWLELTK YALSHAKPLS GLEQWEQNAI
RNASRIAWFD KMNKEGIDII MCPVSFGPAA ISHECEHWAY TAIFNVLDMP GSVFPTGITV
DPQIDAEDTF KPRTEYEARQ RDKYLRAPEK YIDAPINLQL IGRQFRDEEV LAYTKVIASA
VLGE
//
