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P83692

- GANA_THIHE

UniProt

P83692 - GANA_THIHE

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Protein
Arabinogalactan endo-beta-1,4-galactanase
Gene
N/A
Organism
Thielavia heterothallica (Myceliophthora thermophila)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei135 – 1351Proton donor By similarityBy similarity
Active sitei245 – 2451Nucleophile By similarityBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. 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_THIHE.

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

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 912AH → SD: Lowers pH profile by 0.5 units. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Arabinogalactan endo-beta-1,4-galactanase
PRO_0000057706Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi111 – 1111N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86
Helixi12 – 176
Helixi32 – 387
Beta strandi43 – 486
Helixi59 – 7113
Beta strandi75 – 806
Beta strandi83 – 853
Helixi102 – 12221
Beta strandi128 – 1358
Helixi136 – 1383
Helixi150 – 16516
Beta strandi174 – 1807
Helixi185 – 19612
Beta strandi199 – 2013
Helixi203 – 2053
Beta strandi208 – 2125
Beta strandi215 – 2173
Helixi223 – 23715
Beta strandi240 – 2456
Helixi261 – 2633
Helixi270 – 28516
Beta strandi290 – 2967
Helixi301 – 3033
Turni304 – 3074
Beta strandi308 – 3125
Beta strandi320 – 3223
Helixi324 – 3307

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HJSX-ray1.87A/B/C/D1-332[»]
1HJUX-ray2.15A/B/C/D1-332[»]
ProteinModelPortaliP83692.
SMRiP83692. Positions 1-332.

Miscellaneous databases

EvolutionaryTraceiP83692.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 53 family.1 Publication

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

ALTYRGVDWS SVVVEERAGV SYKNTNGNAQ PLENILAANG VNTVRQRVWV    50
NPADGNYNLD YNIAIAKRAK AAGLGVYIDF HYSDTWADPA HQTMPAGWPS 100
DIDNLSWKLY NYTLDAANKL QNAGIQPTIV SIGNEIRAGL LWPTGRTENW 150
ANIARLLHSA AWGIKDSSLS PKPKIMIHLD NGWDWGTQNW WYTNVLKQGT 200
LELSDFDMMG VSFYPFYSSS ATLSALKSSL DNMAKTWNKE IAVVETNWPI 250
SCPNPRYSFP SDVKNIPFSP EGQTTFITNV ANIVSSVSRG VGLFYWEPAW 300
IHNANLGSSC ADNTMFSQSG QALSSLSVFQ RI 332
Length:332
Mass (Da):36,812
Last modified:December 15, 2003 - v1
Checksum:i71CA092FDB1D43DC
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HJS X-ray 1.87 A/B/C/D 1-332 [» ]
1HJU X-ray 2.15 A/B/C/D 1-332 [» ]
ProteinModelPortali P83692.
SMRi P83692. Positions 1-332.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH53. Glycoside Hydrolase Family 53.
mycoCLAPi GAN53A_THIHE.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P83692.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR011683. Glyco_hydro_53.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF07745. Glyco_hydro_53. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum."
    Le Nours J., Ryttersgaard C., Lo Leggio L., Oestergaard P.R., Borchert T.V., Christensen L.L.H., Larsen S.
    Protein Sci. 12:1195-1204(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-111, MUTAGENESIS OF 90-ASP-HIS-91.

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: June 11, 2014
This is version 50 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

External Data

Dasty 3

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