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Protein

Extracellular exo-alpha-L-arabinofuranosidase

Gene

abfB

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. Acts synergistically with the xylanases and binds specifically to xylan. From small arabinoxylo-oligosides (ranging from arabinoxylotriose to arabinoxylohexaose), it liberates arabinose and, after prolonged incubation, the purified enzyme exhibits some xylanolytic activity as well (By similarity).By similarity

Catalytic activityi

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.

Pathwayi: xylan degradation

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Keywords - Ligandi

Lectin

Enzyme and pathway databases

BRENDAi3.2.1.55. 5998.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GH62. Glycoside Hydrolase Family 62.

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular exo-alpha-L-arabinofuranosidase (EC:3.2.1.55)
Short name:
ABF
Alternative name(s):
Arabinosidase
Arabinoxylan arabinofuranohydrolase
Gene namesi
Name:abfB
Ordered Locus Names:SCO5932
ORF Names:SC7H1.02
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 37Sequence analysisAdd BLAST37
ChainiPRO_000000803638 – 475Extracellular exo-alpha-L-arabinofuranosidaseAdd BLAST438

Interactioni

Protein-protein interaction databases

STRINGi100226.SCO5932.

Structurei

Secondary structure

1475
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi184 – 186Combined sources3
Beta strandi198 – 208Combined sources11
Beta strandi211 – 219Combined sources9
Beta strandi224 – 229Combined sources6
Beta strandi232 – 234Combined sources3
Helixi235 – 240Combined sources6
Beta strandi243 – 245Combined sources3
Beta strandi251 – 258Combined sources8
Helixi259 – 261Combined sources3
Beta strandi263 – 281Combined sources19
Beta strandi293 – 296Combined sources4
Beta strandi307 – 314Combined sources8
Beta strandi316 – 324Combined sources9
Beta strandi326 – 336Combined sources11
Helixi337 – 339Combined sources3
Beta strandi349 – 353Combined sources5
Turni356 – 358Combined sources3
Beta strandi361 – 368Combined sources8
Turni369 – 372Combined sources4
Beta strandi374 – 381Combined sources8
Beta strandi383 – 395Combined sources13
Beta strandi401 – 413Combined sources13
Turni414 – 416Combined sources3
Beta strandi426 – 430Combined sources5
Beta strandi432 – 434Combined sources3
Helixi443 – 445Combined sources3
Beta strandi447 – 452Combined sources6
Helixi461 – 463Combined sources3
Beta strandi467 – 473Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WMYX-ray1.40A38-475[»]
3WMZX-ray1.90A38-475[»]
3WN0X-ray1.90A38-475[»]
3WN1X-ray2.00A38-475[»]
3WN2X-ray2.10A38-475[»]
ProteinModelPortaliO54161.
SMRiO54161.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 166Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST128

Sequence similaritiesi

Belongs to the glycosyl hydr olase 62 family.Curated
Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000025219.
InParanoidiO54161.
OMAiWNTELTQ.
OrthoDBiPOG091H0CR4.
PhylomeDBiO54161.

Family and domain databases

InterProiIPR005193. GH62_arabinosidase.
IPR023296. Glyco_hydro_beta-prop.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF03664. Glyco_hydro_62. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O54161-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHRGSLSRGH TSAVLAAVVA ALAALAALLV ATTPAQAAGS GALRGAGSNR
60 70 80 90 100
CLDVLGGSQD DGALLQLYDC WGGTNQQWTS TDTGRLTVYG DKCLDVPGHA
110 120 130 140 150
TAPGTRVQIW SCSGGANQQW RVNSDGTVVG VESGLCLEAA GAGTANGTAV
160 170 180 190 200
QLWTCNGGGN QKWTGLTGTP PTDGTCALPS TYRWSSTGVL AQPKSGWVAL
210 220 230 240 250
KDFTTVTHNG RHLVYGSTSS GSSYGSMVFS PFTNWSDMAS AGQNAMNQAA
260 270 280 290 300
VAPTLFYFAP KNIWVLAYQW GSWPFIYRTS SDPTDPNGWS APQPLFTGSI
310 320 330 340 350
SGSDTGPIDQ TLIADGQNMY LFFAGDNGKI YRASMPIGNF PGNFGSSYTT
360 370 380 390 400
IMSDTKANLF EGVQVYKVQG QNQYLMIVEA MGANGRYFRS FTASSLSGSW
410 420 430 440 450
TPQAASEGNP FAGKANSGAT WTNDISHGDL VRDNPDQTMT VDPCNLQFLY
460 470
QGKSPNAGGD YNSLPWRPGV LTLRR
Length:475
Mass (Da):50,046
Last modified:June 1, 1998 - v1
Checksum:i47E707FE543CA60D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939125 Genomic DNA. Translation: CAA16189.1.
PIRiT35697.
RefSeqiNP_630049.1. NC_003888.3.
WP_011030541.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAA16189; CAA16189; CAA16189.
GeneIDi1101374.
KEGGisco:SCO5932.
PATRICi23741764. VBIStrCoe124346_6029.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939125 Genomic DNA. Translation: CAA16189.1.
PIRiT35697.
RefSeqiNP_630049.1. NC_003888.3.
WP_011030541.1. NC_003888.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WMYX-ray1.40A38-475[»]
3WMZX-ray1.90A38-475[»]
3WN0X-ray1.90A38-475[»]
3WN1X-ray2.00A38-475[»]
3WN2X-ray2.10A38-475[»]
ProteinModelPortaliO54161.
SMRiO54161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO5932.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GH62. Glycoside Hydrolase Family 62.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAA16189; CAA16189; CAA16189.
GeneIDi1101374.
KEGGisco:SCO5932.
PATRICi23741764. VBIStrCoe124346_6029.

Phylogenomic databases

HOGENOMiHOG000025219.
InParanoidiO54161.
OMAiWNTELTQ.
OrthoDBiPOG091H0CR4.
PhylomeDBiO54161.

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.55. 5998.

Family and domain databases

InterProiIPR005193. GH62_arabinosidase.
IPR023296. Glyco_hydro_beta-prop.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF03664. Glyco_hydro_62. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEABF_STRCO
AccessioniPrimary (citable) accession number: O54161
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: November 2, 2016
This is version 113 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, Complete proteome, Reference proteome

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.