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Protein

Probable alpha-galactosidase A

Gene

aglA

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei148NucleophileBy similarity1
Active sitei206Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Probable alpha-galactosidase A (EC:3.2.1.22)
Alternative name(s):
Melibiase A
Gene namesi
Name:aglA
ORF Names:ACLA_016820
OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Taxonomic identifieri344612 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006701 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:ACLA_016820.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000039321318 – 525Probable alpha-galactosidase AAdd BLAST508

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi40 ↔ 72PROSITE-ProRule annotation
Glycosylationi43N-linked (GlcNAc...)Sequence analysis1
Glycosylationi81N-linked (GlcNAc...)Sequence analysis1
Glycosylationi117N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi120 ↔ 150PROSITE-ProRule annotation
Glycosylationi197N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi422 ↔ 434PROSITE-ProRule annotation
Disulfide bondi459 ↔ 472PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliA1CBW8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini402 – 525Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST124

Sequence similaritiesi

Belongs to the glycosyl hydrolase 27 family.Curated
Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000161224.
KOiK07407.
OMAiARHSTDI.
OrthoDBiEOG092C1MJ6.

Family and domain databases

CDDicd14792. GH27. 1 hit.
Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002241. Glyco_hydro_27.
IPR013780. Glyco_hydro_b.
IPR017853. Glycoside_hydrolase_SF.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF16499. Melibiase_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
PRINTSiPR00740. GLHYDRLASE27.
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A1CBW8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHPSMTLLAI LPPLVRASIG NPHLLPTPPM GFNNWARFMC NLNESLFLDT
60 70 80 90 100
AAAMLDTGLH AAGYTRLNLD DCWMASHRAP NGSLPWDPTK FPHSLPWLSA
110 120 130 140 150
QLRSLGFSLG IYQDAGNVTC GGYPGSYGFE ELDAHTFAEW GVDYLKLDGC
160 170 180 190 200
NVSPAGAVSL ADEYRARYAR WHSVLGAMPH PLVFSESAPA YFVDPQNATA
210 220 230 240 250
WYGVMDWVPA YGELARHSTD ILVYEGEGSA WQSIMVNYRY NTLLARYQRP
260 270 280 290 300
GYFNDPDFLI ADHPGLSLVE KRSHFALWAS FGAPLIISAD VPGLSKEVIA
310 320 330 340 350
VLTNADLIRV DQDALGLQAT LASRSEHLDV LTRSLDGGDR LVTILNRGDG
360 370 380 390 400
GLAVKVPVGW MGLQRCAYQA KNLWDGEIQE IEEDIEVQLD SHATEVFRVS
410 420 430 440 450
LPPDCPMVIP TGIVFNTASG NCLTDGEALA FEPCRGQDLQ VWQVEESGIL
460 470 480 490 500
RPLSRTSHCL TAIGDNVVVK PCTGRPGQRW TYHITGNLQN QHTGACLTEG
510 520
TGIDVCGFEL DSQVFGLPSG VDIEA
Length:525
Mass (Da):57,347
Last modified:January 23, 2007 - v1
Checksum:iDBDD564471DEF811
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027049 Genomic DNA. Translation: EAW13236.1.
RefSeqiXP_001274662.1. XM_001274661.1.

Genome annotation databases

EnsemblFungiiCADACLAT00001543; CADACLAP00001524; CADACLAG00001543.
GeneIDi4706882.
KEGGiact:ACLA_016820.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027049 Genomic DNA. Translation: EAW13236.1.
RefSeqiXP_001274662.1. XM_001274661.1.

3D structure databases

ProteinModelPortaliA1CBW8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADACLAT00001543; CADACLAP00001524; CADACLAG00001543.
GeneIDi4706882.
KEGGiact:ACLA_016820.

Organism-specific databases

EuPathDBiFungiDB:ACLA_016820.

Phylogenomic databases

HOGENOMiHOG000161224.
KOiK07407.
OMAiARHSTDI.
OrthoDBiEOG092C1MJ6.

Family and domain databases

CDDicd14792. GH27. 1 hit.
Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002241. Glyco_hydro_27.
IPR013780. Glyco_hydro_b.
IPR017853. Glycoside_hydrolase_SF.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF16499. Melibiase_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
PRINTSiPR00740. GLHYDRLASE27.
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAGALA_ASPCL
AccessioniPrimary (citable) accession number: A1CBW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 50 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

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.