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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: 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)DescriptionActionsGraphical viewLength
Active sitei153Proton donorBy similarity1
Active sitei263NucleophileBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • 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

CAZyiGH53. Glycoside Hydrolase Family 53.
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
Proteomesi
  • UP000000560 Componenti: Chromosome V
  • UP000005890 Componenti: Partially assembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000039495118 – 350Arabinogalactan endo-beta-1,4-galactanase AAdd BLAST333

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi129N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1350
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi20 – 25Combined sources6
Helixi29 – 34Combined sources6
Helixi49 – 55Combined sources7
Beta strandi60 – 65Combined sources6
Helixi76 – 88Combined sources13
Beta strandi92 – 97Combined sources6
Beta strandi100 – 102Combined sources3
Helixi120 – 140Combined sources21
Beta strandi146 – 153Combined sources8
Helixi154 – 156Combined sources3
Beta strandi158 – 160Combined sources3
Turni161 – 163Combined sources3
Helixi168 – 183Combined sources16
Beta strandi192 – 198Combined sources7
Helixi203 – 215Combined sources13
Beta strandi217 – 219Combined sources3
Beta strandi226 – 230Combined sources5
Beta strandi233 – 235Combined sources3
Helixi241 – 255Combined sources15
Beta strandi258 – 263Combined sources6
Helixi279 – 281Combined sources3
Helixi288 – 305Combined sources18
Beta strandi309 – 313Combined sources5
Helixi318 – 320Combined sources3
Turni321 – 324Combined sources4
Beta strandi325 – 329Combined sources5
Turni335 – 337Combined sources3
Helixi342 – 345Combined sources4
Helixi346 – 350Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BF7X-ray2.00A1-350[»]
ProteinModelPortaliQ5B153.
SMRiQ5B153.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 53 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000217077.
InParanoidiQ5B153.
KOiK01224.
OrthoDBiEOG092C2PF8.

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
EAA62820; EAA62820; AN5727.2.
GeneIDi2872012.
KEGGiani:AN5727.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BF7X-ray2.00A1-350[»]
ProteinModelPortaliQ5B153.
SMRiQ5B153.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH53. Glycoside Hydrolase Family 53.
mycoCLAPiGAN53A_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00003335; CADANIAP00003335; CADANIAG00003335.
EAA62820; EAA62820; AN5727.2.
GeneIDi2872012.
KEGGiani:AN5727.2.

Phylogenomic databases

HOGENOMiHOG000217077.
InParanoidiQ5B153.
KOiK01224.
OrthoDBiEOG092C2PF8.

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.
ProtoNetiSearch...

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: November 30, 2016
This is version 66 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.