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Protein

Intracellular endo-alpha-(1->5)-L-arabinanase

Gene

abnB

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of debranched arabinan, linear arabinan and short arabino-oligosaccharides (degree of polymerization from 2 to 8). It exhibits marginal activity toward sugar beet arabinan.1 Publication

Catalytic activityi

Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.1 Publication

Cofactori

Ca2+CuratedNote: Binds 1 Ca2+ ion per subunit.Curated

Pathwayi: L-arabinan degradation

This protein is involved in the pathway L-arabinan degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway L-arabinan degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei27Proton acceptor1 Publication1
Binding sitei27Substrate1
Binding sitei105Substrate; via amide nitrogen1
Sitei147Important for catalytic activity1
Active sitei201Proton donor1 Publication1
Metal bindingi271CalciumSequence analysis1
Sitei271Important for substrate recognitionBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.99. 623.
UniPathwayiUPA00667.

Protein family/group databases

CAZyiGH43. Glycoside Hydrolase Family 43.

Names & Taxonomyi

Protein namesi
Recommended name:
Intracellular endo-alpha-(1->5)-L-arabinanase (EC:3.2.1.99)
Short name:
ABN
Alternative name(s):
Endo-1,5-alpha-L-arabinanase
Gene namesi
Name:abnB
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004221291 – 315Intracellular endo-alpha-(1->5)-L-arabinanaseAdd BLAST315

Expressioni

Inductioni

Transcription is repressed by glucose and by the binding of AraR to the operon promoter. L-arabinose acts as an inducer by inhibiting the binding of AraR to the DNA, thus allowing expression of the gene.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1315
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 14Combined sources3
Beta strandi29 – 33Combined sources5
Beta strandi36 – 44Combined sources9
Beta strandi46 – 63Combined sources18
Helixi71 – 74Combined sources4
Beta strandi82 – 91Combined sources10
Beta strandi94 – 101Combined sources8
Beta strandi109 – 117Combined sources9
Beta strandi129 – 137Combined sources9
Beta strandi141 – 143Combined sources3
Beta strandi149 – 152Combined sources4
Beta strandi158 – 162Combined sources5
Beta strandi169 – 173Combined sources5
Turni176 – 178Combined sources3
Beta strandi188 – 191Combined sources4
Beta strandi194 – 197Combined sources4
Beta strandi200 – 208Combined sources9
Beta strandi211 – 219Combined sources9
Helixi224 – 226Combined sources3
Beta strandi230 – 238Combined sources9
Helixi251 – 253Combined sources3
Beta strandi257 – 260Combined sources4
Beta strandi264 – 277Combined sources14
Beta strandi280 – 289Combined sources10
Turni290 – 294Combined sources5
Beta strandi296 – 305Combined sources10
Beta strandi311 – 313Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CU9X-ray1.06A2-315[»]
3D5YX-ray1.22A2-315[»]
3D5ZX-ray1.90A2-315[»]
3D60X-ray1.90A2-315[»]
3D61X-ray1.95A2-315[»]
ProteinModelPortaliB3EYM8.
SMRiB3EYM8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiB3EYM8.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni144 – 147Substrate binding4
Regioni164 – 166Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the glycosyl hydrolase 43 family.Curated

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR006710. Glyco_hydro_43.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERiPTHR22925. PTHR22925. 1 hit.
PfamiPF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
PIRSFiPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAMiSSF75005. SSF75005. 1 hit.

Sequencei

Sequence statusi: Complete.

B3EYM8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHFHPFGNV NFYEMDWSLK GDLWAHDPVI AKEGSRWYVF HTGSGIQIKT
60 70 80 90 100
SEDGVHWENM GWVFPSLPDW YKQYVPEKDE DHLWAPDICF YNGIYYLYYS
110 120 130 140 150
VSTFGKNTSV IGLATNQTLD PRDPDYEWKD MGPVIHSTAS DNYNAIDPNV
160 170 180 190 200
VFDQEGQPWL SFGSFWSGIQ LIQLDTETMK PAAQAELLTI ASRGEEPNAI
210 220 230 240 250
EAPFIVCRNG YYYLFVSFDF CCRGIESTYK IAVGRSKDIT GPYVDKNGVS
260 270 280 290 300
MMQGGGTILD EGNDRWIGPG HCAVYFSGVS AILVNHAYDA LKNGEPTLQI
310
RPLYWDDEGW PYLSV
Length:315
Mass (Da):35,763
Last modified:July 22, 2008 - v1
Checksum:i86861395D823A044
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ868502 Genomic DNA. Translation: ACE73676.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ868502 Genomic DNA. Translation: ACE73676.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CU9X-ray1.06A2-315[»]
3D5YX-ray1.22A2-315[»]
3D5ZX-ray1.90A2-315[»]
3D60X-ray1.90A2-315[»]
3D61X-ray1.95A2-315[»]
ProteinModelPortaliB3EYM8.
SMRiB3EYM8.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH43. Glycoside Hydrolase Family 43.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00667.
BRENDAi3.2.1.99. 623.

Miscellaneous databases

EvolutionaryTraceiB3EYM8.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR006710. Glyco_hydro_43.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERiPTHR22925. PTHR22925. 1 hit.
PfamiPF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
PIRSFiPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAMiSSF75005. SSF75005. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiIABN_GEOSE
AccessioniPrimary (citable) accession number: B3EYM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2013
Last sequence update: July 22, 2008
Last modified: November 2, 2016
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.