SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P48842

- GANA_ASPAC

UniProt

P48842 - GANA_ASPAC

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Arabinogalactan endo-beta-1,4-galactanase
Gene
gal1
Organism
Aspergillus aculeatus
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.

pH dependencei

Optimum pH is 4.0-4.5.

Temperature dependencei

Optimum temperature is 40-65 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei152 – 1521Proton donor By similarity
Active sitei262 – 2621Nucleophile By similarity

GO - Molecular functioni

  1. arabinogalactan endo-1,4-beta-galactosidase activity Source: UniProtKB-EC
  2. glucosidase activity Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi198 – 1981D → N: Broadens pH profile by 1 unit towards the basic end of the scale. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16161 Publication
Add
BLAST
Chaini17 – 350334Arabinogalactan endo-beta-1,4-galactanase
PRO_0000012221Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi128 – 1281N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 246
Helixi28 – 336
Helixi48 – 558
Beta strandi59 – 646
Helixi75 – 8713
Beta strandi91 – 966
Beta strandi99 – 1013
Helixi119 – 13921
Beta strandi145 – 1528
Helixi153 – 1553
Beta strandi157 – 1593
Turni160 – 1623
Helixi167 – 18216
Beta strandi191 – 1977
Helixi202 – 21413
Beta strandi216 – 2183
Helixi220 – 2223
Beta strandi225 – 2295
Beta strandi232 – 2343
Helixi240 – 25415
Beta strandi258 – 2625
Helixi278 – 2803
Helixi287 – 30216
Beta strandi307 – 3137
Turni321 – 3244
Beta strandi325 – 3295
Turni335 – 3373
Helixi343 – 3486

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FHLX-ray2.30A17-350[»]
1FOBX-ray1.80A17-350[»]
ProteinModelPortaliP48842.
SMRiP48842. Positions 17-350.

Miscellaneous databases

EvolutionaryTraceiP48842.

Family & Domainsi

Sequence similaritiesi

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

MFASLLLAAL PLLTHAALTY RGADISSLLL LEDEGYSYKN LNGQTQALET    50
ILADAGINSI RQRVWVNPSD GSYDLDYNLE LAKRVKAAGM SLYLDLHLSD 100
TWADPSDQTT PSGWSTTDLG TLKWQLYNYT LEVCNTFAEN DIDIEIISIG 150
NEIRAGLLWP LGETSSYSNI GALLHSGAWG VKDSNLATTP KIMIHLDDGW 200
SWDQQNYFYE TVLATGELLS TDFDYFGVSY YPFYSASATL ASLKTSLANL 250
QSTYDKPVVV VETNWPVSCP NPAYAFPSDL SSIPFSVAGQ QEFLEKLAAV 300
VEATTDGLGV YYWEPAWIGN AGLGSSCADN LMVDYTTDEV YESIETLGEL 350
Length:350
Mass (Da):38,423
Last modified:February 1, 1996 - v1
Checksum:i9074249DFAB24CAC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L34599 mRNA. Translation: AAA32692.1.
PIRiS51494.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L34599 mRNA. Translation: AAA32692.1 .
PIRi S51494.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FHL X-ray 2.30 A 17-350 [» ]
1FOB X-ray 1.80 A 17-350 [» ]
ProteinModelPortali P48842.
SMRi P48842. Positions 17-350.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH53. Glycoside Hydrolase Family 53.
mycoCLAPi GAN53A_ASPAC.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P48842.

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. "Expression cloning, purification and characterization of a beta-1,4-galactanase from Aspergillus aculeatus."
    Christgau S., Sandal T., Kofod L.V., Dalboege H.
    Curr. Genet. 27:135-141(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-44.
    Strain: KSM 510.
  2. "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: MUTAGENESIS OF ASP-198.
  3. "Aspergillus aculeatus beta-1,4-galactanase: substrate recognition and relations to other glycoside hydrolases in clan GH-A."
    Ryttersgaard C., Lo Leggio L., Coutinho P.M., Henrissat B., Larsen S.
    Biochemistry 41:15135-15143(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

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: June 11, 2014
This is version 72 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

External Data

Dasty 3

Similar proteinsi