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Protein

Endo-xylogalacturonan hydrolase A

Gene

xghA

Organism
Aspergillus tubingensis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Pectinolytic enzyme involved in the degradation of xylogalacturonan (xga), a galacturonan backbone heavily substituted with xylose, and which is one important component of the hairy regions of pectin. Activity requires a galacturonic acid backbone substituted with xylose.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei228Proton donorBy similarity1
Active sitei251By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiXGH28A_ASPTU.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-xylogalacturonan hydrolase A (EC:3.2.1.-)
Gene namesi
Name:xghA
OrganismiAspergillus tubingensis
Taxonomic identifieri5068 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000039470019 – 406Endo-xylogalacturonan hydrolase AAdd BLAST388

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi278N-linked (GlcNAc...)Sequence analysis1
Glycosylationi301N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1406
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi50 – 60Combined sources11
Beta strandi65 – 68Combined sources4
Beta strandi73 – 76Combined sources4
Beta strandi86 – 92Combined sources7
Beta strandi94 – 98Combined sources5
Helixi102 – 105Combined sources4
Beta strandi109 – 116Combined sources8
Beta strandi118 – 123Combined sources6
Beta strandi125 – 127Combined sources3
Beta strandi130 – 132Combined sources3
Helixi136 – 144Combined sources9
Beta strandi152 – 158Combined sources7
Beta strandi160 – 166Combined sources7
Beta strandi168 – 170Combined sources3
Beta strandi176 – 180Combined sources5
Beta strandi183 – 194Combined sources12
Beta strandi198 – 201Combined sources4
Beta strandi208 – 211Combined sources4
Beta strandi213 – 225Combined sources13
Beta strandi230 – 233Combined sources4
Beta strandi237 – 249Combined sources13
Beta strandi253 – 258Combined sources6
Beta strandi260 – 262Combined sources3
Beta strandi264 – 278Combined sources15
Beta strandi280 – 287Combined sources8
Beta strandi297 – 321Combined sources25
Helixi326 – 331Combined sources6
Beta strandi337 – 350Combined sources14
Beta strandi352 – 354Combined sources3
Beta strandi357 – 362Combined sources6
Beta strandi367 – 376Combined sources10
Beta strandi386 – 391Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C2LX-ray1.75A19-406[»]
ProteinModelPortaliQ9UUZ2.
SMRiQ9UUZ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati183 – 213PbH1 1Add BLAST31
Repeati214 – 257PbH1 2Add BLAST44
Repeati266 – 289PbH1 3Add BLAST24
Repeati299 – 320PbH1 4Add BLAST22
Repeati333 – 375PbH1 5Add BLAST43

Sequence similaritiesi

Belongs to the glycosyl hydrolase 28 family.Curated
Contains 5 PbH1 repeats.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR000743. Glyco_hydro_28.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00295. Glyco_hydro_28. 1 hit.
[Graphical view]
SMARTiSM00710. PbH1. 5 hits.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UUZ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALYRNLYLL ASLGLSSAAP SKVQRAPDSS IHARAVCTPT AGGDSSTDDV
60 70 80 90 100
PAITEALSSC GNGGTIVFPE GSTYYLNSVL DLGSCSDCDI QVEGLLKFAS
110 120 130 140 150
DTDYWSGRTA MISVSNVDGL KLRSLTGSGV IDGNGQDAWD LFASDSSYSR
160 170 180 190 200
PTLLYITGGS NLEISGLRQK NPPNVFNSVK GGATNVVFSN LKMDANSKSD
210 220 230 240 250
NPPKNTDGFD IGESTYVTIT EVTVVNDDDC VAFKPSSNYV TVDTISCTGS
260 270 280 290 300
HGISVGSLGK SSDDSVKNIY VTGATMINST KAAGIKTYPS GGDHGTSTVS
310 320 330 340 350
NVTFNDFTVD NSDYAFQIQS CYGEDDDYCE ENPGNAKLTD IVVSSFSGTT
360 370 380 390 400
SDKYDPVVAN LDCGADGTCG ISISGFDVKA PSGKSEVLCA NTPSDLGVTC

TSGASG
Length:406
Mass (Da):42,071
Last modified:May 1, 2000 - v1
Checksum:i190707D20C9D995E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ249460 mRNA. Translation: CAB65657.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ249460 mRNA. Translation: CAB65657.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C2LX-ray1.75A19-406[»]
ProteinModelPortaliQ9UUZ2.
SMRiQ9UUZ2.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiXGH28A_ASPTU.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR000743. Glyco_hydro_28.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00295. Glyco_hydro_28. 1 hit.
[Graphical view]
SMARTiSM00710. PbH1. 5 hits.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiXGHA_ASPTU
AccessioniPrimary (citable) accession number: Q9UUZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 63 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

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.