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Protein

Arabinoxylan arabinofuranohydrolase

Gene

xynD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves arabinose units from O-2- or O-3-monosubstituted xylose residues, thereby assisting in arabinoxylan (AX) and short-chain arabinoxylo-oligosaccharide (AXOS) degradation. Is more active on wheat bran AXOS than on wheat water-extractable AX and rye water-extractable AX. Does not display endoxylanase, xylosidase or arabinanase activity.1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is 5.6. Stable from pH 4.4 to 7.6.1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius. Thermostable for 40 min from 4 to 45 degrees Celsius.1 Publication

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei50Proton acceptor1
Sitei189Important for catalytic activity1
Active sitei251Proton donor1
Binding sitei314Substrate1
Metal bindingi385Calcium; structural1
Metal bindingi387Calcium; structural1
Metal bindingi409Calcium; structural1
Metal bindingi410Calcium; via carbonyl oxygen; structural1
Metal bindingi506Calcium; structural1
Metal bindingi506Calcium; via carbonyl oxygen; structural1

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

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU18160-MONOMER.
BRENDAi3.2.1.55. 658.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM6. Carbohydrate-Binding Module Family 6.
GH43. Glycoside Hydrolase Family 43.

Names & Taxonomyi

Protein namesi
Recommended name:
Arabinoxylan arabinofuranohydrolase (EC:3.2.1.55)
Short name:
AXH
Alternative name(s):
AXH-m2,3
Short name:
AXH-m23
Alpha-L-arabinofuranosidase
Short name:
AF
Gene namesi
Name:xynD
Ordered Locus Names:BSU18160
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000036082827 – 513Arabinoxylan arabinofuranohydrolaseAdd BLAST487

Proteomic databases

PaxDbiQ45071.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100010001.

Structurei

Secondary structure

1513
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 34Combined sources3
Beta strandi49 – 56Combined sources8
Beta strandi59 – 65Combined sources7
Beta strandi87 – 105Combined sources19
Beta strandi110 – 112Combined sources3
Helixi113 – 116Combined sources4
Beta strandi127 – 136Combined sources10
Beta strandi139 – 148Combined sources10
Beta strandi153 – 160Combined sources8
Beta strandi168 – 171Combined sources4
Beta strandi185 – 187Combined sources3
Beta strandi191 – 194Combined sources4
Beta strandi200 – 205Combined sources6
Helixi216 – 220Combined sources5
Beta strandi225 – 230Combined sources6
Beta strandi234 – 244Combined sources11
Beta strandi249 – 258Combined sources10
Beta strandi261 – 268Combined sources8
Beta strandi270 – 272Combined sources3
Beta strandi282 – 290Combined sources9
Beta strandi296 – 302Combined sources7
Helixi305 – 309Combined sources5
Beta strandi317 – 322Combined sources6
Beta strandi325 – 333Combined sources9
Helixi334 – 340Combined sources7
Beta strandi348 – 353Combined sources6
Beta strandi388 – 394Combined sources7
Beta strandi396 – 399Combined sources4
Beta strandi410 – 413Combined sources4
Beta strandi420 – 427Combined sources8
Turni429 – 431Combined sources3
Beta strandi433 – 441Combined sources9
Beta strandi446 – 454Combined sources9
Beta strandi459 – 465Combined sources7
Beta strandi475 – 480Combined sources6
Beta strandi486 – 495Combined sources10
Beta strandi497 – 500Combined sources4
Beta strandi504 – 512Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C7EX-ray2.00A27-513[»]
3C7FX-ray1.55A27-513[»]
3C7GX-ray2.02A27-513[»]
3C7HX-ray2.00A27-513[»]
3C7OX-ray1.80A27-513[»]
ProteinModelPortaliQ45071.
SMRiQ45071.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ45071.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini382 – 511CBM6PROSITE-ProRule annotationAdd BLAST130

Domaini

The CBM6 domain lost its carbohydrate binding capacity.

Sequence similaritiesi

Belongs to the glycosyl hydrolase 43 family.Curated
Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107SYN. Bacteria.
ENOG410ZVEF. LUCA.
HOGENOMiHOG000292007.
InParanoidiQ45071.
KOiK15921.
OMAiHHAVFNF.
PhylomeDBiQ45071.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
2.60.120.260. 1 hit.
InterProiIPR006584. Cellulose-bd_IV.
IPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR006710. Glyco_hydro_43.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERiPTHR22925. PTHR22925. 2 hits.
PfamiPF03422. CBM_6. 1 hit.
PF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
SMARTiSM00606. CBD_IV. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS51175. CBM6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q45071-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKKCSVCLW ILVLLLSCLS GKSAYAATST TIAKHIGNSN PLIDHHLGAD
60 70 80 90 100
PVALTYNGRV YIYMSSDDYE YNSNGTIKDN SFANLNRVFV ISSADMVNWT
110 120 130 140 150
DHGAIPVAGA NGANGGRGIA KWAGASWAPS IAVKKINGKD KFFLYFANSG
160 170 180 190 200
GGIGVLTADS PIGPWTDPIG KPLVTPSTPG MSGVVWLFDP AVFVDDDGTG
210 220 230 240 250
YLYAGGGVPG VSNPTQGQWA NPKTARVIKL GPDMTSVVGS ASTIDAPFMF
260 270 280 290 300
EDSGLHKYNG TYYYSYCINF GGTHPADKPP GEIGYMTSSS PMGPFTYRGH
310 320 330 340 350
FLKNPGAFFG GGGNNHHAVF NFKNEWYVVY HAQTVSSALF GAGKGYRSPH
360 370 380 390 400
INKLVHNADG SIQEVAANYA GVTQISNLNP YNRVEAETFA WNGRILTEKS
410 420 430 440 450
TAPGGPVNNQ HVTSIQNGDW IAVGNADFGA GGARSFKANV ASTLGGKIEV
460 470 480 490 500
RLDSADGKLV GTLNVPSTGG AQTWREIETA VSGATGVHKV FFVFTGTGTG
510
NLFNFDYWQF TQR
Length:513
Mass (Da):54,498
Last modified:June 1, 1998 - v2
Checksum:i1EBC94AB6CE1490F
GO

Mass spectrometryi

Molecular mass is 52080 Da from positions 27 - 513. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13699.1.
PIRiH69735.
RefSeqiNP_389698.1. NC_000964.3.
WP_003245027.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13699; CAB13699; BSU18160.
GeneIDi936433.
KEGGibsu:BSU18160.
PATRICi18975467. VBIBacSub10457_1925.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13699.1.
PIRiH69735.
RefSeqiNP_389698.1. NC_000964.3.
WP_003245027.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C7EX-ray2.00A27-513[»]
3C7FX-ray1.55A27-513[»]
3C7GX-ray2.02A27-513[»]
3C7HX-ray2.00A27-513[»]
3C7OX-ray1.80A27-513[»]
ProteinModelPortaliQ45071.
SMRiQ45071.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100010001.

Protein family/group databases

CAZyiCBM6. Carbohydrate-Binding Module Family 6.
GH43. Glycoside Hydrolase Family 43.

Proteomic databases

PaxDbiQ45071.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13699; CAB13699; BSU18160.
GeneIDi936433.
KEGGibsu:BSU18160.
PATRICi18975467. VBIBacSub10457_1925.

Phylogenomic databases

eggNOGiENOG4107SYN. Bacteria.
ENOG410ZVEF. LUCA.
HOGENOMiHOG000292007.
InParanoidiQ45071.
KOiK15921.
OMAiHHAVFNF.
PhylomeDBiQ45071.

Enzyme and pathway databases

UniPathwayiUPA00114.
BioCyciBSUB:BSU18160-MONOMER.
BRENDAi3.2.1.55. 658.

Miscellaneous databases

EvolutionaryTraceiQ45071.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
2.60.120.260. 1 hit.
InterProiIPR006584. Cellulose-bd_IV.
IPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR006710. Glyco_hydro_43.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERiPTHR22925. PTHR22925. 2 hits.
PfamiPF03422. CBM_6. 1 hit.
PF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
SMARTiSM00606. CBD_IV. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS51175. CBM6. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYND_BACSU
AccessioniPrimary (citable) accession number: Q45071
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: June 1, 1998
Last modified: November 2, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.