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Protein

Alpha-galactosidase

Gene

agl1

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei46GalactoseCombined sources1
Binding sitei131GalactoseCombined sources1
Binding sitei232GalactoseCombined sources1
Binding sitei249GalactoseCombined sources1
Binding sitei253GalactoseCombined sources1
Binding sitei269Mannose; via carbonyl oxygenCombined sources1
Binding sitei273MannoseCombined sources1
Binding sitei358MannoseCombined sources1

GO - Molecular functioni

  • alpha-galactosidase activity Source: UniProtKB
  • raffinose alpha-galactosidase activity Source: UniProtKB-EC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationSAAS annotationImported, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.22. 6451.

Protein family/group databases

CAZyiGH27. Glycoside Hydrolase Family 27.
mycoCLAPiMEL27A_TRIRE.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-galactosidaseUniRule annotation (EC:3.2.1.22UniRule annotation)
Alternative name(s):
MelibiaseUniRule annotation
Gene namesi
Name:agl1Imported
OrganismiHypocrea jecorina (Trichoderma reesei)Imported
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_500432094728 – 444Alpha-galactosidaseSequence analysisAdd BLAST417

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi51 ↔ 83Combined sources
GlycosylationiCAR_500539008998N-linked (GlcNAc...)Combined sources1
Disulfide bondi131 ↔ 161Combined sources
Disulfide bondi174 ↔ 187Combined sources
GlycosylationiCAR_5005390088184N-linked (GlcNAc...)Combined sources1
GlycosylationiCAR_5005390090242N-linked (GlcNAc...)Combined sources1
GlycosylationiCAR_5005390087361N-linked (GlcNAc...)Combined sources1
Disulfide bondi419 ↔ 441Combined sources

Keywords - PTMi

Disulfide bondUniRule annotationSAAS annotation

Interactioni

Protein-protein interaction databases

STRINGi51453.JGI72632.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SZNX-ray1.54A28-444[»]
1T0OX-ray1.96A28-444[»]
ProteinModelPortaliQ92456.
SMRiQ92456.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92456.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni81 – 82Galactose bindingCombined sources2
Regioni157 – 159Galactose bindingCombined sources3

Sequence similaritiesi

Belongs to the glycosyl hydrolase 27 family.UniRule annotationSAAS annotation

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiKOG2366. Eukaryota.
ENOG410XPF1. LUCA.

Family and domain databases

CDDicd14792. GH27. 1 hit.
Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 2 hits.
InterProiIPR013785. Aldolase_TIM.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_27/36_CS.
IPR013780. Glyco_hydro_b.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF16499. Melibiase_2. 2 hits.
[Graphical view]
PRINTSiPR00740. GLHYDRLASE27.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q92456-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPHSIDRAA RPSVWSGLAL LLSTAHAIVM PDGVTGKVPS LGWNSWNAYH
60 70 80 90 100
CDIDESKFLS AAEVIVSSGL LDAGYNYVNI DDCWSMKDGR VDGHIAVNTT
110 120 130 140 150
RFPDGIDGLA KKVHDLGLKL GIYSTAGTAT CAGYPASLGY EDVDAADFAD
160 170 180 190 200
WGVDYLKYDN CNVPSDWQDE YVACAPDAVQ TGPNGTCSTA LEPNLAPPGY
210 220 230 240 250
DWSTSKSAER FNAMRNALAK QSREIVLSLC IWGVADVFSW GNETGISWRM
260 270 280 290 300
SGDISPEWGS VTHIINMNSF KMNSVGFWGH NDADILEVGN GNLTAAETRT
310 320 330 340 350
HFALWAAMKS PLLIGTDLAQ LSQENIELLK NKHLLAFNQD SVYGQPATPY
360 370 380 390 400
KWGVNPDWTF NYTNPAEYWA GPSSKGHLVL MMNTLDHTVR KEAKWSEIPG
410 420 430 440
LSAGRYEVRD VWTDKSLGCL SSYKTAVAAH DTAVILVGKK CRNW
Length:444
Mass (Da):48,516
Last modified:February 1, 1997 - v1
Checksum:iD7134781CFFD765A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69253 mRNA. Translation: CAA93244.1.
PIRiS74221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69253 mRNA. Translation: CAA93244.1.
PIRiS74221.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SZNX-ray1.54A28-444[»]
1T0OX-ray1.96A28-444[»]
ProteinModelPortaliQ92456.
SMRiQ92456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi51453.JGI72632.

Protein family/group databases

CAZyiGH27. Glycoside Hydrolase Family 27.
mycoCLAPiMEL27A_TRIRE.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2366. Eukaryota.
ENOG410XPF1. LUCA.

Enzyme and pathway databases

BRENDAi3.2.1.22. 6451.

Miscellaneous databases

EvolutionaryTraceiQ92456.

Family and domain databases

CDDicd14792. GH27. 1 hit.
Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 2 hits.
InterProiIPR013785. Aldolase_TIM.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_27/36_CS.
IPR013780. Glyco_hydro_b.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF16499. Melibiase_2. 2 hits.
[Graphical view]
PRINTSiPR00740. GLHYDRLASE27.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQ92456_HYPJE
AccessioniPrimary (citable) accession number: Q92456
Entry historyi
Integrated into UniProtKB/TrEMBL: February 1, 1997
Last sequence update: February 1, 1997
Last modified: November 30, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.