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Protein

Acetylxylan esterase

Gene

axe1

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone.1 Publication

Catalytic activityi

Deacetylation of xylans and xylo-oligosaccharides.

Enzyme regulationi

Inhibited by phenylmethylsulfonyl flouride.

Pathwayi: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei121By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16372.
BRENDAi3.1.1.72. 6451.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
ESTHERihypje-axylest. Acetylxylan_esterase.
mycoCLAPiAXE5A_TRIRE.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylxylan esterase (EC:3.1.1.72)
Gene namesi
Name:axe1
OrganismiHypocrea jecorina (Trichoderma reesei)
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000002077121 – 31Sequence analysisAdd BLAST11
ChainiPRO_000002077232 – 302Acetylxylan esteraseAdd BLAST271

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei32Pyrrolidone carboxylic acid1
Glycosylationi94N-linked (GlcNAc...)Curated1
Disulfide bondi274 ↔ 291By similarity
Disulfide bondi285 ↔ 301By similarity

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiQ99034.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi51453.JGI73632.

Structurei

Secondary structure

1302
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 41Combined sources7
Helixi51 – 53Combined sources3
Helixi54 – 63Combined sources10
Beta strandi67 – 71Combined sources5
Helixi81 – 83Combined sources3
Helixi88 – 109Combined sources22
Beta strandi113 – 120Combined sources8
Helixi122 – 132Combined sources11
Helixi137 – 139Combined sources3
Helixi150 – 155Combined sources6
Beta strandi156 – 163Combined sources8
Beta strandi174 – 177Combined sources4
Helixi195 – 197Combined sources3
Beta strandi198 – 201Combined sources4
Beta strandi207 – 211Combined sources5
Helixi215 – 219Combined sources5
Helixi221 – 236Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QOZX-ray1.90A/B33-238[»]
ProteinModelPortaliQ99034.
SMRiQ99034.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99034.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini266 – 302CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni244 – 266LinkerBy similarityAdd BLAST23

Sequence similaritiesi

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IIT8. Eukaryota.
ENOG4111V6F. LUCA.
KOiK05972.
OMAiNNFHNSC.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR000675. Cutinase/axe.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF01083. Cutinase. 1 hit.
[Graphical view]
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM01110. Cutinase. 1 hit.
SM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q99034-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSVKETLTL LLSQAFLATG SPVDGETVVK RQCPAIHVFG ARETTVSQGY
60 70 80 90 100
GSSATVVNLV IQAHPGTTSE AIVYPACGGQ ASCGGISYAN SVVNGTNAAA
110 120 130 140 150
AAINNFHNSC PDTQLVLVGY SQGAQIFDNA LCGGGDPGEG ITNTAVPLTA
160 170 180 190 200
GAVSAVKAAI FMGDPRNIHG LPYNVGTCTT QGFDARPAGF VCPSASKIKS
210 220 230 240 250
YCDAADPYCC TGNDPNVHQG YGQEYGQQAL AFINSQLSSG GSQPPGGGPT
260 270 280 290 300
STSRPTSTRT GSSPGPTQTH WGQCGGQGWT GPTQCESGTT CQVISQWYSQ

CL
Length:302
Mass (Da):30,754
Last modified:November 1, 1996 - v1
Checksum:iBB6EDCA2971A9F2A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69256 mRNA. Translation: CAA93247.1.
PIRiS71334.

Genome annotation databases

KEGGiag:CAA93247.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69256 mRNA. Translation: CAA93247.1.
PIRiS71334.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QOZX-ray1.90A/B33-238[»]
ProteinModelPortaliQ99034.
SMRiQ99034.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi51453.JGI73632.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
ESTHERihypje-axylest. Acetylxylan_esterase.
mycoCLAPiAXE5A_TRIRE.

Proteomic databases

PRIDEiQ99034.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA93247.

Phylogenomic databases

eggNOGiENOG410IIT8. Eukaryota.
ENOG4111V6F. LUCA.
KOiK05972.
OMAiNNFHNSC.

Enzyme and pathway databases

UniPathwayiUPA00114.
BioCyciMetaCyc:MONOMER-16372.
BRENDAi3.1.1.72. 6451.

Miscellaneous databases

EvolutionaryTraceiQ99034.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR000675. Cutinase/axe.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF01083. Cutinase. 1 hit.
[Graphical view]
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM01110. Cutinase. 1 hit.
SM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAXE1_HYPJE
AccessioniPrimary (citable) accession number: Q99034
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.