ID A0A316YIC7_9BASI Unreviewed; 575 AA.
AC A0A316YIC7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, 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=FA10DRAFT_269423 {ECO:0000313|EMBL:PWN87465.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN87465.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN87465.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN87465.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(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; KZ819640; PWN87465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316YIC7; -.
DR STRING; 215250.A0A316YIC7; -.
DR InParanoid; A0A316YIC7; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000245768; 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; 2.
DR PIRSF; PIRSF001221; Amidase_fungi; 2.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 2.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000245768}.
FT DOMAIN 65..152
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT DOMAIN 167..563
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT REGION 515..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 115
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 245
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
SQ SEQUENCE 575 AA; 63078 MW; 526D98E61DD3E4FF CRC64;
MNAALSRNEG EGEPIRADAQ TTFRSLIEGD RLLTAEELSI VEESDDATQL ADHIARGRRT
CVQVTKVHLK LAALLQQACG PYSEIFFDAA LKRAEELDRR SEKAGRLFGV PISIKAHISM
EGTGSDRGFV FDVLRPEAKR RLVDELEKQG QVEESIISLL RKQAEHLGSS NAPMVDKLLS
EGAIIIAKTR MPQSVVQLDT RSNLHGQTLN PLNMNLSPGG SSGGEAASVS AGATFLGLGT
DIGGSVRQPA SCCGLYGIRP SVGRIAVAGI NSTMPGNEGI IGTAGPFAKS RRDLELMMAI
LASGSHNVDP FLCPPIPWQN TEDVELPKRK LRVGVMYHDG HVEPITPIRR TLAHVVEQLK
ADGRVEIIPF DAEDAGVVAW KLARELYCFM ESGQLIKSLA NLTNEPLVPL TRYICETSPV
KNHSAAESWE LQYARETFKR QFWKRFGSSS SSSSPFGPDA KIDVLLCPAG AQVAPRPGKI
WYWGYTSLFN LTDLPGVVFP AKNFVADSKA DLQYEGREKG RTQSNEALDK QNKEEYERNR
EVFDGAPVGL QLIGHRFKEE TLLKSLELIE HAMKH
//
