ID A0A1L9V409_ASPGL Unreviewed; 301 AA.
AC A0A1L9V409;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=feruloyl esterase {ECO:0000256|ARBA:ARBA00013091};
DE EC=3.1.1.73 {ECO:0000256|ARBA:ARBA00013091};
DE AltName: Full=Ferulic acid esterase A {ECO:0000256|ARBA:ARBA00041313};
GN ORFNames=ASPGLDRAFT_182276 {ECO:0000313|EMBL:OJJ78674.1};
OS Aspergillus glaucus CBS 516.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Aspergillus.
OX NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ78674.1, ECO:0000313|Proteomes:UP000184300};
RN [1] {ECO:0000313|Proteomes:UP000184300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73; Evidence={ECO:0000256|ARBA:ARBA00034075};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. FaeA family.
CC {ECO:0000256|ARBA:ARBA00037991}.
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; KV878930; OJJ78674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9V409; -.
DR STRING; 1160497.A0A1L9V409; -.
DR VEuPathDB; FungiDB:ASPGLDRAFT_182276; -.
DR OrthoDB; 179907at2759; -.
DR Proteomes; UP000184300; Unassembled WGS sequence.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00519; Lipase_3; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR InterPro; IPR005592; Mono/diacylglycerol_lipase_N.
DR PANTHER; PTHR46640:SF1; LIPASE_3 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR46640; TRIACYLGLYCEROL LIPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G06510)-RELATED; 1.
DR Pfam; PF03893; Lipase3_N; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022487};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000184300};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..301
FT /note="feruloyl esterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009887823"
FT DOMAIN 8..78
FT /note="Mono-/di-acylglycerol lipase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03893"
FT DOMAIN 102..232
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
SQ SEQUENCE 301 AA; 32698 MW; A9A2FFEBD963F2E0 CRC64;
MHLSLAILSF LAVCSHAIPL NPQARDVPAD ELSQFNFWVE YAAASYCHDN YVAKTGDKLT
CWADNCPQVE QADTEILYDF SNTTATDTSG FVALDTTTKA IVIAFRGSYS VRNWIADATF
IHTDPKLCDG CLAELGFWSS WTLVRHSIME TLNHTVSEHP DYEVVVVGHS LGAAVATLAA
TDIRSKGHPS AKLYAYASPR VANSALAKHI TAQDGNYRFS HIDDPVPKLP LLSMGYVHVS
PEYYISSATN ATVHTGDIEV LEGEVNFQGN TGTGPPLLTA FPAHNWYFGK TDGCKGPGLP
L
//
