FAEC1_ASPCL
ID FAEC1_ASPCL Reviewed; 272 AA.
AC A1C9D4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Probable feruloyl esterase C;
DE EC=3.1.1.73;
DE AltName: Full=Ferulic acid esterase C-1;
DE Flags: Precursor;
GN Name=faeC-1; ORFNames=ACLA_055050;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the
CC feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-
CC galactose ester bond in pectin. Active against paranitrophenyl-acetate,
CC methyl ferulate and wheat arabinoxylan (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the faeC family. {ECO:0000305}.
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DR EMBL; DS027048; EAW13458.1; -; Genomic_DNA.
DR RefSeq; XP_001274884.1; XM_001274883.1.
DR AlphaFoldDB; A1C9D4; -.
DR SMR; A1C9D4; -.
DR STRING; 5057.CADACLAP00005103; -.
DR ESTHER; aspcl-faec1; FaeC.
DR EnsemblFungi; EAW13458; EAW13458; ACLA_055050.
DR GeneID; 4706967; -.
DR KEGG; act:ACLA_055050; -.
DR VEuPathDB; FungiDB:ACLA_055050; -.
DR eggNOG; ENOG502SMEI; Eukaryota.
DR HOGENOM; CLU_027551_2_0_1; -.
DR OMA; SSGCGKQ; -.
DR OrthoDB; 1257904at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030600; F:feruloyl esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR043595; FaeB/C/D.
DR InterPro; IPR034429; FaeC.
DR PANTHER; PTHR38050; PTHR38050; 1.
DR PANTHER; PTHR38050:SF1; PTHR38050:SF1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..272
FT /note="Probable feruloyl esterase C"
FT /id="PRO_0000394935"
SQ SEQUENCE 272 AA; 28480 MW; 2E1B4C577A17819D CRC64;
MLPTILYSAI LALSALTPSA LAETRSSGCG KHPSLANGVI HLNGREYILK LPDRYDNNHA
YHLVFGLHWR GGNMQNVANG ESIQPWYGLE TRAQGSTIFI APNGKNAGWA NNGGEDVAFI
DAIIKQVEAD LCVDQSSRFA TGFSWGGGMS YSLACSRAKQ FKAVSVLSGG VISGCDGGHD
PIAYLGIHGI NDGVLPFNGG VGLAQKFVQN NGCQQANIGA PPSGSKSSVR TDFKGCSKPV
SFIAYDGGHD SAPLGVGSSL APDATWKFFM AA
