ID A0A2H3DHY8_ARMGA Unreviewed; 568 AA.
AC A0A2H3DHY8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, 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=ARMGADRAFT_68817 {ECO:0000313|EMBL:PBK94831.1};
OS Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=47427 {ECO:0000313|EMBL:PBK94831.1, ECO:0000313|Proteomes:UP000217790};
RN [1] {ECO:0000313|Proteomes:UP000217790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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; KZ293653; PBK94831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3DHY8; -.
DR STRING; 47427.A0A2H3DHY8; -.
DR InParanoid; A0A2H3DHY8; -.
DR OMA; EYHAPIS; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000217790; 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:SF10; ACETAMIDASE; 1.
DR PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR Pfam; PF01425; Amidase; 1.
DR PIRSF; PIRSF001221; Amidase_fungi; 2.
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:UP000217790}.
FT DOMAIN 61..545
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 108
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 207
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 204..207
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
SQ SEQUENCE 568 AA; 62828 MW; EE9B7B56D30768FB CRC64;
MASFLSHWKA CHVKQEERKK RIEDLDPAYH EPLSNKDAEI LGRPIADLVA SVQSGACDSD
ILVAYSKQAL KAHAKTNCLS EVMIASAETW AKECNKKGPL AGVPVSLKDS VGVKGWDSTI
GYSAWVGQPI QEDGPLVRLL RDAGAVPFVK TTIPITLLSF ESSSDLFGRT TNPHNPAYSP
GGSSGGEAAL LAFGGSRIGL GTDVAGSVRT PSHYSGVYTI RSSTTRFPKL GGVTSIPGQE
GVAAVCSPMA RTLADLETFW KAVVSQKPWD YDHTCLNLPW RDMDVSKKSL KWGVMWDDGV
VQPSPACKRA LYSVVETLQN HGHEVFTMWV WPPFLPSGAY TMASRPAPSP YEGLQIAFQL
LLADGGKTVM KPFQMGETND PGVSQARIMF SLPRWARRLY VWYLRYLRGD EIYAGLVEGC
YEKSITEYWP LVAQREAYRR RWFDMWNEQN LDFLLTVPNA LPAVPHGGMR EGFKSCGYTF
LFNLLDYTAG VLPVTHVNEK LDVLKGFKPR NAVEAGAYKD YDSVKMDGLP VGVQIVGKRL
EEEKVMEGMK LIERLLKEDG KAYELLNV
//