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Q5B153

- GANA_EMENI

UniProt

Q5B153 - GANA_EMENI

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Protein

Arabinogalactan endo-beta-1,4-galactanase A

Gene

galA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Endogalactanase involved in the degradation of plant cell wall polysaccharides, and more particularly of hairy regions of pectin.1 Publication

Catalytic activityi

The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic linkages in type I arabinogalactans.

pH dependencei

Optimum pH is 5.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei153 – 1531Proton donorBy similarity
Active sitei263 – 2631NucleophileBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. pectin catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Protein family/group databases

mycoCLAPiGAN53A_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Arabinogalactan endo-beta-1,4-galactanase A (EC:3.2.1.89)
Alternative name(s):
Endo-1,4-beta-galactanase A
Short name:
Galactanase A
Gene namesi
Name:galA
ORF Names:AN5727
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome V

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 350333Arabinogalactan endo-beta-1,4-galactanase APRO_0000394951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 256
Helixi29 – 346
Helixi49 – 557
Beta strandi60 – 656
Helixi76 – 8813
Beta strandi92 – 976
Beta strandi100 – 1023
Helixi120 – 14021
Beta strandi146 – 1538
Helixi154 – 1563
Beta strandi158 – 1603
Turni161 – 1633
Helixi168 – 18316
Beta strandi192 – 1987
Helixi203 – 21513
Beta strandi217 – 2193
Beta strandi226 – 2305
Beta strandi233 – 2353
Helixi241 – 25515
Beta strandi258 – 2636
Helixi279 – 2813
Helixi288 – 30518
Beta strandi309 – 3135
Helixi318 – 3203
Turni321 – 3244
Beta strandi325 – 3295
Turni335 – 3373
Helixi342 – 3454
Helixi346 – 3505

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BF7X-ray2.00A1-350[»]
ProteinModelPortaliQ5B153.
SMRiQ5B153. Positions 18-350.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 53 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3867.
HOGENOMiHOG000217077.
InParanoidiQ5B153.
KOiK01224.
OrthoDBiEOG7CG78S.

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.

Q5B153-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MILSSLLPLS LVTLTSAALT YRGADISSLL IEEDSGVAYK NLNGETQAFE
60 70 80 90 100
LILANNGVNS IRQRIWVNPS DGSYNLEYNL ELAKRVQDAG MSVYLDLHLS
110 120 130 140 150
DTWADPGDQA TPSGWSTTDI DTLAWQVYNY TLDVCNTFAE NNVAVEIVSI
160 170 180 190 200
GNEIRNGLLH PLGSTDHYDN IARLLHSGAW GVKDSSLSTT PKILFHLDNG
210 220 230 240 250
WDWDAQKYFY DTVLATGTLL STDFDLIGVS YYPFYNADAT LSSLKTSLTN
260 270 280 290 300
LKSNYGKNVL VVETDWPVQC SSPEYAFPSD LSSIPFSADG QETFLGRLAD
310 320 330 340 350
TLEDVGGVGI YYWEPGWVDN AGLGSSCEDN LMVDWRDRTV RESISVFGDL
Length:350
Mass (Da):38,572
Last modified:June 15, 2010 - v2
Checksum:i5FF6131E86E5CA3F
GO

Sequence cautioni

The sequence CBF81324.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence EAA62820.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ490498 mRNA. Translation: ABF50874.1.
AACD01000098 Genomic DNA. Translation: EAA62820.1. Sequence problems.
BN001305 Genomic DNA. Translation: CBF81324.1. Sequence problems.
RefSeqiXP_663331.1. XM_658239.1.

Genome annotation databases

EnsemblFungiiCADANIAT00003335; CADANIAP00003335; CADANIAG00003335.
GeneIDi2872012.
KEGGiani:AN5727.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ490498 mRNA. Translation: ABF50874.1 .
AACD01000098 Genomic DNA. Translation: EAA62820.1 . Sequence problems.
BN001305 Genomic DNA. Translation: CBF81324.1 . Sequence problems.
RefSeqi XP_663331.1. XM_658239.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BF7 X-ray 2.00 A 1-350 [» ]
ProteinModelPortali Q5B153.
SMRi Q5B153. Positions 18-350.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

mycoCLAPi GAN53A_EMENI.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00003335 ; CADANIAP00003335 ; CADANIAG00003335 .
GeneIDi 2872012.
KEGGi ani:AN5727.2.

Phylogenomic databases

eggNOGi COG3867.
HOGENOMi HOG000217077.
InParanoidi Q5B153.
KOi K01224.
OrthoDBi EOG7CG78S.

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

« Hide 'large scale' publications
  1. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
    Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
    Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiGANA_EMENI
AccessioniPrimary (citable) accession number: Q5B153
Secondary accession number(s): C8VFL3, Q1HFS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: October 29, 2014
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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