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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei148 – 1481NucleophileBy similarity
Active sitei206 – 2061Proton donorBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. raffinose alpha-galactosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
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
ProteomesiUP000006701: Unassembled WGS sequence

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 525508Probable alpha-galactosidase APRO_0000393213Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 72PROSITE-ProRule annotation
Glycosylationi43 – 431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi120 ↔ 150PROSITE-ProRule annotation
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi422 ↔ 434PROSITE-ProRule annotation
Disulfide bondi459 ↔ 472PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5057.CADACLAP00001524.

Structurei

3D structure databases

ProteinModelPortaliA1CBW8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini402 – 525124Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

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

eggNOGiNOG68897.
HOGENOMiHOG000161224.
KOiK07407.
OMAiARHSTDI.
OrthoDBiEOG7SR4WK.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF02065. Melibiase. 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...

Protein-protein interaction databases

STRINGi5057.CADACLAP00001524.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiNOG68897.
HOGENOMiHOG000161224.
KOiK07407.
OMAiARHSTDI.
OrthoDBiEOG7SR4WK.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF02065. Melibiase. 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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

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: January 7, 2015
This is version 41 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

External Data

Dasty 3

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 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.