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Q45071

- XYND_BACSU

UniProt

Q45071 - XYND_BACSU

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Protein

Arabinoxylan arabinofuranohydrolase

Gene

xynD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501Proton acceptor
Sitei189 – 1891Important for catalytic activity
Active sitei251 – 2511Proton donor
Binding sitei314 – 3141Substrate
Metal bindingi385 – 3851Calcium; structural
Metal bindingi387 – 3871Calcium; structural
Metal bindingi409 – 4091Calcium; structural
Metal bindingi410 – 4101Calcium; via carbonyl oxygen; structural
Metal bindingi506 – 5061Calcium; structural
Metal bindingi506 – 5061Calcium; via carbonyl oxygen; structural

GO - Molecular functioni

  1. alpha-L-arabinofuranosidase activity Source: UniProtKB-EC
  2. carbohydrate binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-UniPathway
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. 700.
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
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU18160. [Micado]

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 513487Arabinoxylan arabinofuranohydrolasePRO_0000360828Add
BLAST

Proteomic databases

PaxDbiQ45071.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU18160.

Structurei

Secondary structure

1
513
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 343
Beta strandi49 – 568
Beta strandi59 – 657
Beta strandi87 – 10519
Beta strandi110 – 1123
Helixi113 – 1164
Beta strandi127 – 13610
Beta strandi139 – 14810
Beta strandi153 – 1608
Beta strandi168 – 1714
Beta strandi185 – 1873
Beta strandi191 – 1944
Beta strandi200 – 2056
Helixi216 – 2205
Beta strandi225 – 2306
Beta strandi234 – 24411
Beta strandi249 – 25810
Beta strandi261 – 2688
Beta strandi270 – 2723
Beta strandi282 – 2909
Beta strandi296 – 3027
Helixi305 – 3095
Beta strandi317 – 3226
Beta strandi325 – 3339
Helixi334 – 3407
Beta strandi348 – 3536
Beta strandi388 – 3947
Beta strandi396 – 3994
Beta strandi410 – 4134
Beta strandi420 – 4278
Turni429 – 4313
Beta strandi433 – 4419
Beta strandi446 – 4549
Beta strandi459 – 4657
Beta strandi475 – 4806
Beta strandi486 – 49510
Beta strandi497 – 5004
Beta strandi504 – 5129

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 27-513.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ45071.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini382 – 511130CBM6PROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG5498.
HOGENOMiHOG000292007.
InParanoidiQ45071.
KOiK15921.
OMAiSPHINKL.
OrthoDBiEOG6GXTPP.
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. 1 hit.
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:
EMBL
GenBank
DDBJ
Links Updated
AL009126 Genomic DNA. Translation: CAB13699.1.
PIRiH69735.
RefSeqiNP_389698.1. NC_000964.3.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL009126 Genomic DNA. Translation: CAB13699.1 .
PIRi H69735.
RefSeqi NP_389698.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3C7E X-ray 2.00 A 27-513 [» ]
3C7F X-ray 1.55 A 27-513 [» ]
3C7G X-ray 2.02 A 27-513 [» ]
3C7H X-ray 2.00 A 27-513 [» ]
3C7O X-ray 1.80 A 27-513 [» ]
ProteinModelPortali Q45071.
SMRi Q45071. Positions 27-513.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU18160.

Protein family/group databases

CAZyi CBM6. Carbohydrate-Binding Module Family 6.
GH43. Glycoside Hydrolase Family 43.

Proteomic databases

PaxDbi Q45071.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13699 ; CAB13699 ; BSU18160 .
GeneIDi 936433.
KEGGi bsu:BSU18160.
PATRICi 18975467. VBIBacSub10457_1925.

Organism-specific databases

GenoListi BSU18160. [Micado ]

Phylogenomic databases

eggNOGi COG5498.
HOGENOMi HOG000292007.
InParanoidi Q45071.
KOi K15921.
OMAi SPHINKL.
OrthoDBi EOG6GXTPP.
PhylomeDBi Q45071.

Enzyme and pathway databases

UniPathwayi UPA00114 .
BioCyci BSUB:BSU18160-MONOMER.
BRENDAi 3.2.1.55. 700.

Miscellaneous databases

EvolutionaryTracei Q45071.

Family and domain databases

Gene3Di 2.115.10.20. 1 hit.
2.60.120.260. 1 hit.
InterProi IPR006584. Cellulose-bd_IV.
IPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR006710. Glyco_hydro_43.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view ]
PANTHERi PTHR22925. PTHR22925. 1 hit.
Pfami PF03422. CBM_6. 1 hit.
PF04616. Glyco_hydro_43. 1 hit.
[Graphical view ]
SMARTi SM00606. CBD_IV. 1 hit.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEi PS51175. CBM6. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "Proteome analysis of Bacillus subtilis extracellular proteins: a two-dimensional protein electrophoretic study."
    Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.
    Microbiology 146:65-75(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-37, SUBCELLULAR LOCATION.
    Strain: 168.
  3. "Recombinant expression and characterization of XynD from Bacillus subtilis subsp. subtilis ATCC 6051: a GH 43 arabinoxylan arabinofuranohydrolase."
    Bourgois T.M., Van Craeyveld V., Van Campenhout S., Courtin C.M., Delcour J.A., Robben J., Volckaert G.
    Appl. Microbiol. Biotechnol. 75:1309-1317(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  4. "Structural analysis of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase in complex with xylotetraose reveals a different binding mechanism compared with other members of the same family."
    Vandermarliere E., Bourgois T.M., Winn M.D., van Campenhout S., Volckaert G., Delcour J.A., Strelkov S.V., Rabijns A., Courtin C.M.
    Biochem. J. 418:39-47(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 27-513 IN COMPLEXES WITH XYLOTRIOSE; XYLOTETRAOSE; ARABINOXYLO-OLIGOSACCHARIDES AND CELLOTETRAOSE.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.

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: October 29, 2014
This is version 92 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

External Data

Dasty 3