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Protein

Feruloyl esterase B

Gene

ESTA

Organism
Piromyces equi
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in degradation of plant cell walls. Hydrolyzes of the feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl-galactose and feruloyl-arabinose ester bonds in pectin.1 Publication

Catalytic activityi

Feruloyl-polysaccharide + H2O = ferulate + polysaccharide.

Enzyme regulationi

Inhibited by the specific serine esterase inhibitor AEBSF.

GO - Molecular functioni

  • feruloyl esterase activity Source: UniProtKB

GO - Biological processi

  • cell wall macromolecule catabolic process Source: UniProtKB
  • pectin catabolic process Source: UniProtKB
  • xylan catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

BRENDAi3.1.1.73. 4866.

Protein family/group databases

ESTHERipireq-faeb. Esterase_phb.
mycoCLAPiFAE1B_PIREQ.

Names & Taxonomyi

Protein namesi
Recommended name:
Feruloyl esterase B (EC:3.1.1.73)
Alternative name(s):
Cinnamoyl ester hydrolase
Esterase A
Short name:
EstA
Ferulic acid esterase B
Gene namesi
Name:ESTA
OrganismiPiromyces equi
Taxonomic identifieri99929 [NCBI]
Taxonomic lineageiEukaryotaFungiNeocallimastigomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaePiromyces

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 536516Feruloyl esterase BPRO_0000021230Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi65 – 651N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Component of the multienzyme cellulase-hemicellulase complex.

Structurei

3D structure databases

ProteinModelPortaliQ9Y871.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 5939CBM10PROSITE-ProRule annotationAdd
BLAST
Repeati78 – 90131Add
BLAST
Repeati91 – 103132Add
BLAST
Repeati104 – 116133Add
BLAST
Repeati117 – 129134Add
BLAST
Repeati134 – 146135Add
BLAST
Repeati151 – 163136Add
BLAST
Repeati164 – 176137Add
BLAST
Repeati181 – 193138Add
BLAST
Repeati194 – 206139Add
BLAST
Repeati211 – 2231310Add
BLAST
Repeati224 – 2361311Add
BLAST
Repeati237 – 2491312Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 5938Cellulose-bindingAdd
BLAST
Regioni78 – 24917212 X 13 AA repeats of N-Q-G-G-G-M-[PQ]-W-G-D-F-G-GAdd
BLAST
Regioni257 – 536280CatalyticAdd
BLAST

Sequence similaritiesi

Contains 1 CBM10 (carbohydrate binding type-10) domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
3.90.1220.10. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002883. CBM10/Dockerin_dom.
IPR009034. Dockerin_dom_fun.
[Graphical view]
PfamiPF02013. CBM_10. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
SSF64571. SSF64571. 1 hit.
PROSITEiPS51763. CBM10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y871-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTSIVLSIV ALFLTSKASA DCWSERLGWP CCSDSNAEVI YVDDDGDWGV
60 70 80 90 100
ENNDWCGIQK EEENNNSWDM GDWNQGGNQG GGMPWGDFGG NQGGGMQWGD
110 120 130 140 150
FGGNQGGGMP WGDFGGNQGG GMPWGDFGGN QGGNQGGGMP WGDFGGNQGG
160 170 180 190 200
NQGGGMPWGD FGGNQGGGMQ WGDFGGNQGG NQGGGMPWGD FGGNQGGGMQ
210 220 230 240 250
WGDFGGNQGG NQGGGMPWGD FGGNQGGGMQ WGDFGGNQGG GMQWGDFGGN
260 270 280 290 300
QGGNQDWGNQ GGNSGPTVEY STDVDCSGKT LKSNTNLNIN GRKVIVKFPS
310 320 330 340 350
GFTGDKAAPL LINYHPIMGS ASQWESGSQT AKAALNDGAI VAFMDGAQGP
360 370 380 390 400
MGQAWNVGPC CTDADDVQFT RNFIKEITSK ACVDPKRIYA AGFSMGGGMS
410 420 430 440 450
NYAGCQLADV IAAAAPSAFD LAKEIVDGGK CKPARPFPIL NFRGTQDNVV
460 470 480 490 500
MYNGGLSQVV QGKPITFMGA KNNFKEWAKM NGCTGEPKQN TPGNNCEMYE
510 520 530
NCKGGVKVGL CTINGGGHAE GDGKMGWDFV KQFSLP
Length:536
Mass (Da):55,540
Last modified:November 1, 1999 - v1
Checksum:i74ECCED78D769F84
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF164516 mRNA. Translation: AAD45376.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF164516 mRNA. Translation: AAD45376.1.

3D structure databases

ProteinModelPortaliQ9Y871.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERipireq-faeb. Esterase_phb.
mycoCLAPiFAE1B_PIREQ.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.1.73. 4866.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
3.90.1220.10. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002883. CBM10/Dockerin_dom.
IPR009034. Dockerin_dom_fun.
[Graphical view]
PfamiPF02013. CBM_10. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
SSF64571. SSF64571. 1 hit.
PROSITEiPS51763. CBM10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFAEB_PIREQ
AccessioniPrimary (citable) accession number: Q9Y871
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 1, 1999
Last modified: May 11, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.