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P48842

- GANA_ASPAC

UniProt

P48842 - GANA_ASPAC

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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 donorBy similarity
Active sitei262 – 2621NucleophileBy 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 PublicationAdd
BLAST
Chaini17 – 350334Arabinogalactan endo-beta-1,4-galactanasePRO_0000012221Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 246Combined sources
Helixi28 – 336Combined sources
Helixi48 – 558Combined sources
Beta strandi59 – 646Combined sources
Helixi75 – 8713Combined sources
Beta strandi91 – 966Combined sources
Beta strandi99 – 1013Combined sources
Helixi119 – 13921Combined sources
Beta strandi145 – 1528Combined sources
Helixi153 – 1553Combined sources
Beta strandi157 – 1593Combined sources
Turni160 – 1623Combined sources
Helixi167 – 18216Combined sources
Beta strandi191 – 1977Combined sources
Helixi202 – 21413Combined sources
Beta strandi216 – 2183Combined sources
Helixi220 – 2223Combined sources
Beta strandi225 – 2295Combined sources
Beta strandi232 – 2343Combined sources
Helixi240 – 25415Combined sources
Beta strandi258 – 2625Combined sources
Helixi278 – 2803Combined sources
Helixi287 – 30216Combined sources
Beta strandi307 – 3137Combined sources
Turni321 – 3244Combined sources
Beta strandi325 – 3295Combined sources
Turni335 – 3373Combined sources
Helixi343 – 3486Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FHLX-ray2.30A17-350[»]
1FOBX-ray1.80A17-350[»]
ProteinModelPortaliP48842.
SMRiP48842. Positions 17-350.
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 .
PIRi S51494.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: October 29, 2014
This is version 74 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