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Protein

Arabinoxylan arabinofuranohydrolase

Gene

xynD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -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 Publication1
Sitei189Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate1 Publication1
Active sitei251Proton donor1 Publication1
Binding sitei314Substrate1 Publication1
Metal bindingi385Calcium; structural1 Publication1
Metal bindingi387Calcium; structural1 Publication1
Metal bindingi409Calcium; structural1 Publication1
Metal bindingi410Calcium; via carbonyl oxygen; structural1 Publication1
Metal bindingi506Calcium; structural1 Publication1
Metal bindingi506Calcium; via carbonyl oxygen; structural1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradation
LigandCalcium, 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

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
PRIDEiQ45071

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107SYN Bacteria
ENOG410ZVEF LUCA
HOGENOMiHOG000292007
InParanoidiQ45071
KOiK15921
OMAiNNEIDPT
PhylomeDBiQ45071

Family and domain databases

Gene3Di2.115.10.20, 1 hit
2.60.120.260, 1 hit
InterProiView protein in InterPro
IPR006584 Cellulose-bd_IV
IPR005084 CMB_fam6
IPR008979 Galactose-bd-like_sf
IPR006710 Glyco_hydro_43
IPR023296 Glyco_hydro_beta-prop_sf
PfamiView protein in Pfam
PF03422 CBM_6, 1 hit
PF04616 Glyco_hydro_43, 1 hit
SMARTiView protein in SMART
SM00606 CBD_IV, 1 hit
SUPFAMiSSF49785 SSF49785, 1 hit
SSF75005 SSF75005, 1 hit
PROSITEiView protein in PROSITE
PS51175 CBM6, 1 hit

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
PATRICifig|224308.179.peg.1980

Similar proteinsi

Entry informationi

Entry nameiXYND_BACSU
AccessioniPrimary (citable) accession number: Q45071
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: June 1, 1998
Last modified: May 23, 2018
This is version 110 of the entry and version 2 of the sequence. See 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
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Main funding by: National Institutes of Health