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Protein

Arabinogalactan endo-beta-1,4-galactanase

Gene

gal1

Organism
Aspergillus aculeatus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic linkages in type I arabinogalactans.

pH dependencei

Optimum pH is 4.0-4.5.

Temperature dependencei

Optimum temperature is 40-65 degrees Celsius.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei152Proton donorBy similarity1
Active sitei262NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH53. Glycoside Hydrolase Family 53.
mycoCLAPiGAN53A_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
OrganismiAspergillus aculeatus
Taxonomic identifieri5053 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi198D → N: Broadens pH profile by 1 unit towards the basic end of the scale. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 161 PublicationAdd BLAST16
ChainiPRO_000001222117 – 350Arabinogalactan endo-beta-1,4-galactanaseAdd BLAST334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi128N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1350
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 24Combined sources6
Helixi28 – 33Combined sources6
Helixi48 – 55Combined sources8
Beta strandi59 – 64Combined sources6
Helixi75 – 87Combined sources13
Beta strandi91 – 96Combined sources6
Beta strandi99 – 101Combined sources3
Helixi119 – 139Combined sources21
Beta strandi145 – 152Combined sources8
Helixi153 – 155Combined sources3
Beta strandi157 – 159Combined sources3
Turni160 – 162Combined sources3
Helixi167 – 182Combined sources16
Beta strandi191 – 197Combined sources7
Helixi202 – 214Combined sources13
Beta strandi216 – 218Combined sources3
Helixi220 – 222Combined sources3
Beta strandi225 – 229Combined sources5
Beta strandi232 – 234Combined sources3
Helixi240 – 254Combined sources15
Beta strandi258 – 262Combined sources5
Helixi278 – 280Combined sources3
Helixi287 – 302Combined sources16
Beta strandi307 – 313Combined sources7
Turni321 – 324Combined sources4
Beta strandi325 – 329Combined sources5
Turni335 – 337Combined sources3
Helixi343 – 348Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FHLX-ray2.30A17-350[»]
1FOBX-ray1.80A17-350[»]
ProteinModelPortaliP48842.
SMRiP48842.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48842.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 53 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR011683. Glyco_hydro_53.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF07745. Glyco_hydro_53. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P48842-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:350
Mass (Da):38,423
Last modified:February 1, 1996 - v1
Checksum:i9074249DFAB24CAC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34599 mRNA. Translation: AAA32692.1.
PIRiS51494.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34599 mRNA. Translation: AAA32692.1.
PIRiS51494.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FHLX-ray2.30A17-350[»]
1FOBX-ray1.80A17-350[»]
ProteinModelPortaliP48842.
SMRiP48842.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH53. Glycoside Hydrolase Family 53.
mycoCLAPiGAN53A_ASPAC.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP48842.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR011683. Glyco_hydro_53.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF07745. Glyco_hydro_53. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGANA_ASPAC
AccessioniPrimary (citable) accession number: P48842
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 2, 2016
This is version 78 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

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.