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P83691

- GANA_HUMIN

UniProt

P83691 - GANA_HUMIN

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Protein

Arabinogalactan endo-beta-1,4-galactanase

Gene
N/A
Organism
Humicola insolens (Soft-rot fungus)
Status
Reviewed - 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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei135 – 1351Proton donorBy similarity
Active sitei245 – 2451NucleophileBy 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_HUMIN.

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
OrganismiHumicola insolens (Soft-rot fungus)
Taxonomic identifieri34413 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Arabinogalactan endo-beta-1,4-galactanasePRO_0000057705Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1
332
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 – 12322
Beta strandi129 – 1357
Beta strandi139 – 1424
Turni143 – 1453
Helixi150 – 16516
Beta strandi174 – 1807
Helixi185 – 19814
Beta strandi199 – 2013
Helixi203 – 2053
Beta strandi208 – 2125
Helixi223 – 23715
Beta strandi240 – 2456
Helixi261 – 2633
Helixi270 – 28617
Beta strandi290 – 2967
Helixi301 – 3033
Turni304 – 3074
Beta strandi308 – 3125
Beta strandi320 – 3223
Helixi324 – 3274
Helixi328 – 3314

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HJQX-ray2.55A1-332[»]
ProteinModelPortaliP83691.
SMRiP83691. Positions 1-332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83691.

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.

P83691-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
ALQYKGVDWS SVMVEERAGV RYKNVNGQEK PLEYILAENG VNMVRQRVWV
60 70 80 90 100
NPWDGNYNLD YNIQLARRAK AAGLGLYINF HYSDTWADPA HQTTPAGWPS
110 120 130 140 150
DINNLAWKLY NYTLDSMNRF ADAGIQVDIV SIGNEITQGL LWPLGKTNNW
160 170 180 190 200
YNIARLLHSA AWGVKDSRLN PKPKIMVHLD NGWNWDTQNW WYTNVLSQGP
210 220 230 240 250
FEMSDFDMMG VSFYPFYSAS ATLDSLRRSL NNMVSRWGKE VAVVETNWPT
260 270 280 290 300
SCPYPRYQFP ADVRNVPFSA AGQTQYIQSV ANVVSSVSKG VGLFYWEPAW
310 320 330
IHNANLGSSC ADNTMFTPSG QALSSLSVFH RI
Length:332
Mass (Da):37,659
Last modified:December 15, 2003 - v1
Checksum:iF6DA01D0F24CA702
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HJQ X-ray 2.55 A 1-332 [» ]
ProteinModelPortali P83691.
SMRi P83691. Positions 1-332.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH53. Glycoside Hydrolase Family 53.
mycoCLAPi GAN53A_HUMIN.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P83691.

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 (2.6 ANGSTROMS), CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-111.

Entry informationi

Entry nameiGANA_HUMIN
AccessioniPrimary (citable) accession number: P83691
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 15, 2003
Last modified: October 1, 2014
This is version 51 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 6.5-9.5 with optimum of 8.5; 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