FAEB_PIREQ
ID FAEB_PIREQ Reviewed; 536 AA.
AC Q9Y871;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Feruloyl esterase B;
DE EC=3.1.1.73;
DE AltName: Full=Cinnamoyl ester hydrolase;
DE AltName: Full=Esterase A;
DE Short=EstA;
DE AltName: Full=Ferulic acid esterase B;
DE Flags: Precursor;
GN Name=ESTA;
OS Piromyces equi.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces; unclassified Piromyces.
OX NCBI_TaxID=99929;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=10493932; DOI=10.1042/bj3430215;
RA Fillingham I.J., Kroon P.A., Williamson G., Gilbert H.J., Hazlewood G.P.;
RT "A modular cinnamoyl ester hydrolase from the anaerobic fungus Piromyces
RT equi acts synergistically with xylanase and is part of a multiprotein
RT cellulose-binding cellulase-hemicellulase complex.";
RL Biochem. J. 343:215-224(1999).
CC -!- FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes of
CC the feruloyl-arabinose ester bond in arabinoxylans as well as the
CC feruloyl-galactose and feruloyl-arabinose ester bonds in pectin.
CC {ECO:0000269|PubMed:10493932}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73;
CC -!- ACTIVITY REGULATION: Inhibited by the specific serine esterase
CC inhibitor AEBSF.
CC -!- SUBUNIT: Component of the multienzyme cellulase-hemicellulase complex.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; AF164516; AAD45376.1; -; mRNA.
DR AlphaFoldDB; Q9Y871; -.
DR SMR; Q9Y871; -.
DR CLAE; FAE1B_PIREQ; -.
DR ESTHER; pireq-faeb; Esterase_phb.
DR BRENDA; 3.1.1.73; 4866.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0030600; F:feruloyl esterase activity; IDA:UniProtKB.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IDA:UniProtKB.
DR GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
DR GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR Gene3D; 3.90.1220.10; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002883; CBM10/Dockerin_dom.
DR InterPro; IPR009034; Dockerin_dom_fun_sf.
DR InterPro; IPR043595; FaeB/C/D.
DR PANTHER; PTHR38050; PTHR38050; 1.
DR Pfam; PF02013; CBM_10; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF64571; SSF64571; 1.
DR PROSITE; PS51763; CBM10; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycoprotein; Hydrolase;
KW Polysaccharide degradation; Repeat; Secreted; Serine esterase; Signal;
KW Xylan degradation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..536
FT /note="Feruloyl esterase B"
FT /id="PRO_0000021230"
FT DOMAIN 21..59
FT /note="CBM10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT REPEAT 78..90
FT /note="1"
FT REPEAT 91..103
FT /note="2"
FT REPEAT 104..116
FT /note="3"
FT REPEAT 117..129
FT /note="4"
FT REPEAT 134..146
FT /note="5"
FT REPEAT 151..163
FT /note="6"
FT REPEAT 164..176
FT /note="7"
FT REPEAT 181..193
FT /note="8"
FT REPEAT 194..206
FT /note="9"
FT REPEAT 211..223
FT /note="10"
FT REPEAT 224..236
FT /note="11"
FT REPEAT 237..249
FT /note="12"
FT REGION 22..59
FT /note="Cellulose-binding"
FT REGION 78..249
FT /note="12 X 13 AA repeats of N-Q-G-G-G-M-[PQ]-W-G-D-F-G-G"
FT REGION 203..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..536
FT /note="Catalytic"
FT COMPBIAS 248..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 536 AA; 55540 MW; 74ECCED78D769F84 CRC64;
MKTSIVLSIV ALFLTSKASA DCWSERLGWP CCSDSNAEVI YVDDDGDWGV ENNDWCGIQK
EEENNNSWDM GDWNQGGNQG GGMPWGDFGG NQGGGMQWGD FGGNQGGGMP WGDFGGNQGG
GMPWGDFGGN QGGNQGGGMP WGDFGGNQGG NQGGGMPWGD FGGNQGGGMQ WGDFGGNQGG
NQGGGMPWGD FGGNQGGGMQ WGDFGGNQGG NQGGGMPWGD FGGNQGGGMQ WGDFGGNQGG
GMQWGDFGGN QGGNQDWGNQ GGNSGPTVEY STDVDCSGKT LKSNTNLNIN GRKVIVKFPS
GFTGDKAAPL LINYHPIMGS ASQWESGSQT AKAALNDGAI VAFMDGAQGP MGQAWNVGPC
CTDADDVQFT RNFIKEITSK ACVDPKRIYA AGFSMGGGMS NYAGCQLADV IAAAAPSAFD
LAKEIVDGGK CKPARPFPIL NFRGTQDNVV MYNGGLSQVV QGKPITFMGA KNNFKEWAKM
NGCTGEPKQN TPGNNCEMYE NCKGGVKVGL CTINGGGHAE GDGKMGWDFV KQFSLP
