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Protein

Arabinogalactan endo-beta-1,4-galactanase

Gene
N/A
Organism
Thielavia heterothallica (Myceliophthora thermophila)
Status
Reviewed-Annotation score: Annotation score: 4 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei135Proton donorBy similarity1
Active sitei245NucleophileBy similarity1

GO - Molecular functioni

  • arabinogalactan endo-1,4-beta-galactosidase activity Source: UniProtKB-EC
  • glucosidase activity Source: InterPro
  • hydrolase activity, hydrolyzing O-glycosyl compounds Source: UniProtKB
  • polysaccharide binding Source: UniProtKB

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • cell wall macromolecule catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH53. Glycoside Hydrolase Family 53.
mycoCLAPiGAN53A_MYCTH.

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
OrganismiThielavia heterothallica (Myceliophthora thermophila)
Taxonomic identifieri78579 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeMyceliophthora

Subcellular locationi

GO - Cellular componenti

  • extraorganismal space Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi90 – 91AH → SD: Lowers pH profile by 0.5 units. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000577061 – 332Arabinogalactan endo-beta-1,4-galactanaseAdd BLAST332

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi111N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP83692.

Structurei

Secondary structure

1332
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Helixi12 – 17Combined sources6
Helixi32 – 38Combined sources7
Beta strandi43 – 48Combined sources6
Helixi59 – 71Combined sources13
Beta strandi75 – 80Combined sources6
Beta strandi83 – 85Combined sources3
Helixi102 – 122Combined sources21
Beta strandi128 – 135Combined sources8
Helixi136 – 138Combined sources3
Helixi150 – 165Combined sources16
Beta strandi174 – 180Combined sources7
Helixi185 – 196Combined sources12
Beta strandi199 – 201Combined sources3
Helixi203 – 205Combined sources3
Beta strandi208 – 212Combined sources5
Beta strandi215 – 217Combined sources3
Helixi223 – 237Combined sources15
Beta strandi240 – 245Combined sources6
Helixi261 – 263Combined sources3
Helixi270 – 285Combined sources16
Beta strandi290 – 296Combined sources7
Helixi301 – 303Combined sources3
Turni304 – 307Combined sources4
Beta strandi308 – 312Combined sources5
Beta strandi320 – 322Combined sources3
Helixi324 – 330Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HJSX-ray1.87A/B/C/D1-332[»]
1HJUX-ray2.15A/B/C/D1-332[»]
ProteinModelPortaliP83692.
SMRiP83692.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83692.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 53 family.1 Publication

Phylogenomic databases

eggNOGiENOG410IFS4. Eukaryota.
COG3867. LUCA.

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.

P83692-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ALTYRGVDWS SVVVEERAGV SYKNTNGNAQ PLENILAANG VNTVRQRVWV
60 70 80 90 100
NPADGNYNLD YNIAIAKRAK AAGLGVYIDF HYSDTWADPA HQTMPAGWPS
110 120 130 140 150
DIDNLSWKLY NYTLDAANKL QNAGIQPTIV SIGNEIRAGL LWPTGRTENW
160 170 180 190 200
ANIARLLHSA AWGIKDSSLS PKPKIMIHLD NGWDWGTQNW WYTNVLKQGT
210 220 230 240 250
LELSDFDMMG VSFYPFYSSS ATLSALKSSL DNMAKTWNKE IAVVETNWPI
260 270 280 290 300
SCPNPRYSFP SDVKNIPFSP EGQTTFITNV ANIVSSVSRG VGLFYWEPAW
310 320 330
IHNANLGSSC ADNTMFSQSG QALSSLSVFQ RI
Length:332
Mass (Da):36,812
Last modified:December 15, 2003 - v1
Checksum:i71CA092FDB1D43DC
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HJSX-ray1.87A/B/C/D1-332[»]
1HJUX-ray2.15A/B/C/D1-332[»]
ProteinModelPortaliP83692.
SMRiP83692.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH53. Glycoside Hydrolase Family 53.
mycoCLAPiGAN53A_MYCTH.

Proteomic databases

PRIDEiP83692.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IFS4. Eukaryota.
COG3867. LUCA.

Miscellaneous databases

EvolutionaryTraceiP83692.

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_THIHE
AccessioniPrimary (citable) accession number: P83692
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 15, 2003
Last modified: November 2, 2016
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Has a pH range of 5.5-8.5 with optimum of 7.0; and a temperature optimum of 65 degrees Celsius at pH 6.5.1 Publication

Keywords - Technical termi

3D-structure

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.