ID A0A365N9N8_GIBIN Unreviewed; 557 AA.
AC A0A365N9N8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN ORFNames=FPRO05_02126 {ECO:0000313|EMBL:RBA17402.1};
OS Gibberella intermedia (Bulb rot disease fungus) (Fusarium proliferatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=948311 {ECO:0000313|EMBL:RBA17402.1, ECO:0000313|Proteomes:UP000251714};
RN [1] {ECO:0000313|EMBL:RBA17402.1, ECO:0000313|Proteomes:UP000251714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITEM 2341 {ECO:0000313|EMBL:RBA17402.1,
RC ECO:0000313|Proteomes:UP000251714};
RA Almiman B.F., Shittu T.A., Muthumeenakshi S., Baroncelli R.,
RA Sreenivasaprasada S.;
RT "Genome sequence of the mycotoxigenic crop pathogen Fusarium proliferatum,
RT strain ITEM 2341 from Date Palm.";
RL Submitted (DEC-2017) 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:RBA17402.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PKMI01000017; RBA17402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365N9N8; -.
DR Proteomes; UP000251714; 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}.
FT DOMAIN 90..543
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 144
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 241
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 238..241
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
SQ SEQUENCE 557 AA; 60662 MW; FBCD8B46F18B1750 CRC64;
MQVNNPVPVP KGTPEHEAKR ASVLKALSDK VPADFCLGPE FFKDTPLDVT KVPSTCGLLT
DEEVSITEDY DATGLAEVIA RRKYTSVVVA RAFCKRAIIA HQLTCCLTQW FYDEAIQQAT
KLDEYLAEHG TTIGPLHGVP VSIKDHIPLA GTFASLGILA TAEYDQRDSP LPAVLRQAGA
VFYCKTNQPQ ALMHGESDSP WGRALNPYNT TLTSGGSSGG EGALIAIKGS VLGIGTDIGG
SIRIPSAFNG IYGYKPTSGI LSTRDLVHGP MVAELTILAN AGPMCRSARD MDLFMRIQLA
TKPHIRDLTL VPTTWTGLST QLGLTLGRPL KVGIMRHDGF IQPQPPLKRA LSWAGTVLSD
SRLSGLIEVK PFLPYGVKQA WDEIRQAYSP DGGIPSHNAI LATGEPIYPL TEWIWKTAAP
KGMLTAAEMA YVRKACLDFR HSFAEDWERQ DVDVILCPTG VGPATTHDTN FYLMYTALWN
YLDCPGLVFP TGLKVEEGEE YDADYKPLGP ECAHVKDLWE SGNFKGAPIS LQLVGRRYHD
NQLFGALKLL QEALGLQ
//
