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UniProtKB - P48842 (GANA_ASPAC)
Protein
Arabinogalactan endo-beta-1,4-galactanase
Gene
gal1
Organism
Aspergillus aculeatus
Status
Functioni
Catalytic activityi
- The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic linkages in type I arabinogalactans. EC:3.2.1.89
pH dependencei
Optimum pH is 4.0-4.5.
Temperature dependencei
Optimum temperature is 40-65 degrees Celsius.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 152 | Proton donorBy similarity | 1 | |
Active sitei | 262 | NucleophileBy similarity | 1 |
GO - Molecular functioni
- arabinogalactan endo-1,4-beta-galactosidase activity Source: UniProtKB-EC
- glucosidase activity Source: InterPro
GO - Biological processi
- metabolic process Source: UniProtKB-KW
Keywordsi
Molecular function | Glycosidase, Hydrolase |
Protein family/group databases
CAZyi | GH53, Glycoside Hydrolase Family 53 |
CLAEi | GAN53A_ASPAC |
Names & Taxonomyi
Protein namesi | Recommended name: Arabinogalactan endo-beta-1,4-galactanase (EC:3.2.1.89)Alternative name(s): Endo-1,4-beta-galactanase Short name: Galactanase |
Gene namesi | Name:gal1 |
Organismi | Aspergillus aculeatus |
Taxonomic identifieri | 5053 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Circumdati |
Organism-specific databases
VEuPathDBi | FungiDB:ASPACDRAFT_78476 |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 198 | D → N: Broadens pH profile by 1 unit towards the basic end of the scale. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 16 | 1 PublicationAdd BLAST | 16 | |
ChainiPRO_0000012221 | 17 – 350 | Arabinogalactan endo-beta-1,4-galactanaseAdd BLAST | 334 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 128 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Post-translational modificationi
Glycosylated.
Keywords - PTMi
GlycoproteinStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P48842 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P48842 |
Family & Domainsi
Sequence similaritiesi
Belongs to the glycosyl hydrolase 53 family.Curated
Keywords - Domaini
SignalFamily and domain databases
InterProi | View protein in InterPro IPR011683, Glyco_hydro_53 IPR017853, Glycoside_hydrolase_SF |
PANTHERi | PTHR34983, PTHR34983, 1 hit |
Pfami | View protein in Pfam PF07745, Glyco_hydro_53, 1 hit |
SUPFAMi | SSF51445, SSF51445, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P48842-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MFASLLLAAL PLLTHAALTY RGADISSLLL LEDEGYSYKN LNGQTQALET
60 70 80 90 100
ILADAGINSI RQRVWVNPSD GSYDLDYNLE LAKRVKAAGM SLYLDLHLSD
110 120 130 140 150
TWADPSDQTT PSGWSTTDLG TLKWQLYNYT LEVCNTFAEN DIDIEIISIG
160 170 180 190 200
NEIRAGLLWP LGETSSYSNI GALLHSGAWG VKDSNLATTP KIMIHLDDGW
210 220 230 240 250
SWDQQNYFYE TVLATGELLS TDFDYFGVSY YPFYSASATL ASLKTSLANL
260 270 280 290 300
QSTYDKPVVV VETNWPVSCP NPAYAFPSDL SSIPFSVAGQ QEFLEKLAAV
310 320 330 340 350
VEATTDGLGV YYWEPAWIGN AGLGSSCADN LMVDYTTDEV YESIETLGEL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L34599 mRNA Translation: AAA32692.1 |
PIRi | S51494 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L34599 mRNA Translation: AAA32692.1 |
PIRi | S51494 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1FHL | X-ray | 2.30 | A | 17-350 | [»] | |
1FOB | X-ray | 1.80 | A | 17-350 | [»] | |
6Q3R | X-ray | 2.69 | A/B | 17-350 | [»] | |
SMRi | P48842 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
CAZyi | GH53, Glycoside Hydrolase Family 53 |
CLAEi | GAN53A_ASPAC |
Organism-specific databases
VEuPathDBi | FungiDB:ASPACDRAFT_78476 |
Miscellaneous databases
EvolutionaryTracei | P48842 |
Family and domain databases
InterProi | View protein in InterPro IPR011683, Glyco_hydro_53 IPR017853, Glycoside_hydrolase_SF |
PANTHERi | PTHR34983, PTHR34983, 1 hit |
Pfami | View protein in Pfam PF07745, Glyco_hydro_53, 1 hit |
SUPFAMi | SSF51445, SSF51445, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | GANA_ASPAC | |
Accessioni | P48842Primary (citable) accession number: P48842 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1996 |
Last sequence update: | February 1, 1996 | |
Last modified: | September 29, 2021 | |
This is version 89 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families