Q4WVZ3

PR
Gene name
aglA (AFUA_5G13830)
Protein name
Probable alpha-galactosidase A
Names
Melibiase A
Species
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
KEGG Pathway
afm:AFUA_5G13830
EC number
3.2.1.22: Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-59 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q4WVZ3

Entry ID Method Resolution Chain Position Source
AF-Q4WVZ3-F1 Predicted AlphaFoldDB

No variants for Q4WVZ3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q4WVZ3

No associated diseases with Q4WVZ3

2 regional properties for Q4WVZ3

Type Name Position InterPro Accession
domain Ricin B, lectin domain 416 - 524 IPR000772
domain Alpha galactosidase, C-terminal beta sandwich domain 332 - 404 IPR041233

Functions

Description
EC Number 3.2.1.22 Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds
Subcellular Localization
  • Secreted
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

3 GO annotations of molecular function

Name Definition
alpha-galactosidase activity Catalysis of the hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase.
carbohydrate binding Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
raffinose alpha-galactosidase activity Catalysis of the reaction: raffinose + H2O = alpha-D-galactose + sucrose.

3 GO annotations of biological process

Name Definition
glycoside catabolic process The chemical reactions and pathways resulting in the breakdown of glycosides, compounds in which a glycosyl group is substituted into a hydroxyl, thiol or selenol group in another compound.
glycosylceramide catabolic process The chemical reactions and pathways resulting in the breakdown of glycosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of a monosaccharide (or derivative) by a ceramide group.
oligosaccharide metabolic process The chemical reactions and pathways involving oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDTTKSLLST LIAIMIPLSL GSVSSPNLLP TPPMGFNNWA RFMCDLNETL FLETASAMIS
70 80 90 100 110 120
TGLLEAGYNR VNLDDCWMAY DRAADSSLQW NTTKFPHGIP WLARHLKAQG FHVGIYEDAG
130 140 150 160 170 180
NLTCGGYPGS FGHEALDAQT FAAWGIDYLK LDGCNVFPEH SRTLEEEYKA RYAHWHSILK
190 200 210 220 230 240
QMHHPLIFSE SAPAYFADPA NLTSWYEVMD WVPAFGELAR HSTDILVYVG EGSAWDSIMV
250 260 270 280 290 300
NYRYNTLLAR YQRPGYINDP DFLIPDHPGL TLEEKRSQFA LWASFSAPLI VSAYIPGLSS
310 320 330 340 350 360
EELAILRNEE LIRVDQDVLG LQATLASRGL EVDVLTRSLE GGDRLLTVLN RGDGVAVVSV
370 380 390 400 410 420
PVEWMGLQRG CPYVVKNLWD GEVQVLEEEI VIRLNSHATQ VYRIALPDEC STVIPTGIVF
430 440 450 460 470 480
NTASGNCLTD ENGERVGFEA CRGSETQIWQ VSELGYLRPL SRTSHCLTGG SQASVQLCTE
490 500 510 520 530
QKNQQWAYAI TGILKNEHTE MCLTEGTGIS QCGFERDSQV FGLPSGVDIK PS