FAEB_MYCTT
ID FAEB_MYCTT Reviewed; 291 AA.
AC G2QND5;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Feruloyl esterase B;
DE EC=3.1.1.73;
DE AltName: Full=Cinnamoyl esterase;
DE AltName: Full=Ferulic acid esterase B;
DE Short=FAEB;
DE Flags: Precursor;
GN Name=Fae1a; ORFNames=MYCTH_96478;
OS Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS (Sporotrichum thermophile).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX NCBI_TaxID=573729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799;
RX PubMed=21964414; DOI=10.1038/nbt.1976;
RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA Tsang A.;
RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT Myceliophthora thermophila and Thielavia terrestris.";
RL Nat. Biotechnol. 29:922-927(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF SER-136.
RX PubMed=22012339; DOI=10.1007/s00253-011-3612-9;
RA Topakas E., Moukouli M., Dimarogona M., Christakopoulos P.;
RT "Expression, characterization and structural modelling of a feruloyl
RT esterase from the thermophilic fungus Myceliophthora thermophila.";
RL Appl. Microbiol. Biotechnol. 94:399-411(2012).
CC -!- FUNCTION: Feruloyl esterase which acts in synergy with xylanases in
CC degradation of plant cell walls. Hydrolyzes the ester linkage of
CC hydroxycinnamic acids (ferulic acid (FA) and p-coumaric acid) and
CC diferulates present in plant cell walls. Is active on substrates
CC containing ferulic acid ester linked to the C-5 and C-2 linkages of
CC arabinofuranose, while it was found capable of de-esterifying
CC acetylated glucuronoxylans. Efficiently releases ferulic acid (FA) from
CC destarched wheat bran when incubated with an M3 xylanase.
CC {ECO:0000269|PubMed:22012339}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73; Evidence={ECO:0000269|PubMed:22012339};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.27 mM for methyl ferulate (MFA) {ECO:0000269|PubMed:22012339};
CC KM=0.26 mM for methyl p-coumarate (MpCA)
CC {ECO:0000269|PubMed:22012339};
CC KM=0.18 mM for methyl caffeate (MCA) {ECO:0000269|PubMed:22012339};
CC KM=0.21 mM for methyl sinapate (MSA) {ECO:0000269|PubMed:22012339};
CC KM=2.29 mM for nitrophenyl-5-O-trans-feruloyl-alpha-L-
CC arabinofuranoside {ECO:0000269|PubMed:22012339};
CC KM=2.79 mM for nitrophenyl-2-O-trans-feruloyl-alpha-L-
CC arabinofuranoside {ECO:0000269|PubMed:22012339};
CC KM=2.33 mM for ethyl ferulate {ECO:0000269|PubMed:22012339};
CC KM=1.14 mM for n-propyl ferulate {ECO:0000269|PubMed:22012339};
CC KM=1.40 mM for iso-propyl ferulate {ECO:0000269|PubMed:22012339};
CC KM=0.74 mM for n-butyl ferulate {ECO:0000269|PubMed:22012339};
CC KM=0.65 mM for iso-butyl ferulate {ECO:0000269|PubMed:22012339};
CC KM=0.74 mM for 2-butyl ferulate {ECO:0000269|PubMed:22012339};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:22012339};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:22012339};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family.
CC Feruloyl esterase type B subfamily. {ECO:0000305}.
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DR EMBL; CP003008; AEO62008.1; -; Genomic_DNA.
DR RefSeq; XP_003667253.1; XM_003667205.1.
DR AlphaFoldDB; G2QND5; -.
DR SMR; G2QND5; -.
DR ESTHER; myctt-faeb; Esterase_phb.
DR EnsemblFungi; AEO62008; AEO62008; MYCTH_96478.
DR GeneID; 11509804; -.
DR KEGG; mtm:MYCTH_96478; -.
DR VEuPathDB; FungiDB:MYCTH_96478; -.
DR eggNOG; ENOG502QTDU; Eukaryota.
DR HOGENOM; CLU_027551_1_1_1; -.
DR InParanoid; G2QND5; -.
DR OrthoDB; 1169544at2759; -.
DR BRENDA; 3.1.1.73; 5542.
DR Proteomes; UP000007322; Chromosome 7.
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; IPR010126; Esterase_phb.
DR Pfam; PF10503; Esterase_PHB; 1.
DR SUPFAM; SSF53474; SSF53474; 2.
DR TIGRFAMs; TIGR01840; esterase_phb; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycoprotein; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Serine esterase;
KW Signal; Xylan degradation.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..291
FT /note="Feruloyl esterase B"
FT /id="PRO_0000419269"
FT ACT_SITE 136
FT /note="Charge relay system"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 136
FT /note="S->A: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:22012339"
SQ SEQUENCE 291 AA; 31372 MW; 5CD9B663A8D6D025 CRC64;
MLVRSFLGFA VLAATCLAAS LQEVTEFGDN PTNIQMYIYV PDQLDTNPPV IVALHPCGGS
AQQWFSGTQL PSYADDNGFI LIYPSTPHMS NCWDIQNPDT LTHGQGGDAL GIVSMVNYTL
DKHSGDSSRV YAMGFSSGGM MTNQLAGSYP DVFEAGAVYS GVAFGCAAGA ESATPFSPNQ
TCAQGLQKTA QEWGDFVRNA YAGYTGRRPR MQIFHGLEDT LVRPQCAEEA LKQWSNVLGV
ELTQEVSGVP SPGWTQKIYG DGTQLQGFFG QGIGHQSTVN EQQLLQWFGL I
