ID S0EG99_GIBF5 Unreviewed; 553 AA.
AC S0EG99;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN ORFNames=FFUJ_09358 {ECO:0000313|EMBL:CCT73819.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT73819.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
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; HF679031; CCT73819.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EG99; -.
DR STRING; 1279085.S0EG99; -.
DR EnsemblFungi; CCT73819; CCT73819; FFUJ_09358.
DR VEuPathDB; FungiDB:FFUJ_09358; -.
DR HOGENOM; CLU_009600_9_2_1; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000016800; Chromosome 9.
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:SF8; AMIDASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR Pfam; PF01425; Amidase; 2.
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:UP000016800}.
FT DOMAIN 79..373
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT DOMAIN 424..536
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 134
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 191
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 553 AA; 60586 MW; 71A8DE44680775EA CRC64;
MDENSWETRA AVKRAATLDK IPSEWRLSSE DLEHAHSQRD ITGSFIERFL DEETASITSL
KTVEILNAVS EQELTTMKVV RAFCQRAAVA HQINNCLHEI FFDQAFERAQ YLDEYFTKHG
KALGPLHGLP ISLKDQFHVK GVDTTMGYVG WIGGNLGIDS DKTYTVESHI VTELLSLGAV
LYCKTSLPQT LLFGETKNNI IGQTLNPINQ NLSCGGSSGG EGALMALGGS SVGVGTDIGG
SLRIPAGFCG IFSIKPTSNR LSYRDVANTN PGQDTYRSTI GFMGTSIDAL EVVFKAILGT
EPWMKDPAVI PIPFRKDVME SYRRRSDEKG NAKSGERPLK MGVFWCDGMV GLHPPVLRGL
TVVVDALKKA GHKGGFLGAD GAHDIHQHLN RSGEPLIPDL QDGLNLETPT ELLKYQDLTI
QGLEFERQYS DYWNSTADSD GQIVDAVLMP VAPHAAVIPG KFYHGAYTDA MNLTNYTAVV
IPTIRADKRI DVFDEGYEPL GEIDRKNWQA YDADLYDGAP VGVQIVGRKF EEEKCLAIAR
IVQAVVESAI KTG
//
