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Protein

Endo-1,4-beta-xylanase C

Gene

xynC

Organism
Paenibacillus barcinonensis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Endoxylanase with high hydrolytic activity on birchwood and oat spelt xylan. Xylotetraose, xylotriose, xylobiose and xylose are the main products from birchwood xylan hydrolysis. Shows increasing activity on xylo-oligosaccharides of increasing length. Displays very low hydrolytic activity on Avicel, carboxymethylcellulose (CMC) and p-nitrophenyl-beta-xylopyranoside. Also shows transxylosidase activity, allowing the formation of xylo-oligosaccharides of higher degreee of polymerization than the starting substrate.1 Publication

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.1 Publication

pH dependencei

Optimum pH is 5. Retains at least 50% of its maximum activity between pH 4.5 and 8.0. Is not active at pH values below 4.5, while at least 35% of maximum activity is found in the pH range 8.5-11.0.1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius. Is only stable at 55 degrees Celsius or lower temperatures. Retains more than 77% activity after 2 hours incubation at 55 degrees Celsius and pH 7.1 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 sitei502Proton donorBy similarity1
Active sitei556By similarity1
Active sitei620NucleophilePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
CBM9. Carbohydrate-Binding Module Family 9.
GH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase C (EC:3.2.1.8)
Short name:
Xylanase C
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase C
Gene namesi
Name:xynC
OrganismiPaenibacillus barcinonensis
Taxonomic identifieri198119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
ChainiPRO_000037142032 – 1086Endo-1,4-beta-xylanase CAdd BLAST1055

Structurei

Secondary structure

11086
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 41Combined sources5
Beta strandi45 – 47Combined sources3
Beta strandi52 – 56Combined sources5
Beta strandi58 – 64Combined sources7
Beta strandi67 – 70Combined sources4
Beta strandi72 – 76Combined sources5
Beta strandi84 – 88Combined sources5
Turni90 – 92Combined sources3
Beta strandi98 – 107Combined sources10
Beta strandi114 – 123Combined sources10
Beta strandi129 – 133Combined sources5
Beta strandi138 – 140Combined sources3
Beta strandi142 – 144Combined sources3
Beta strandi146 – 152Combined sources7
Beta strandi158 – 168Combined sources11
Beta strandi173 – 184Combined sources12
Beta strandi201 – 203Combined sources3
Beta strandi216 – 218Combined sources3
Beta strandi220 – 226Combined sources7
Beta strandi229 – 238Combined sources10
Beta strandi248 – 250Combined sources3
Helixi252 – 254Combined sources3
Beta strandi260 – 268Combined sources9
Beta strandi271 – 286Combined sources16
Beta strandi294 – 304Combined sources11
Beta strandi309 – 316Combined sources8
Helixi320 – 322Combined sources3
Beta strandi324 – 332Combined sources9
Helixi338 – 340Combined sources3
Helixi344 – 346Combined sources3
Beta strandi349 – 358Combined sources10
Helixi371 – 375Combined sources5
Beta strandi378 – 385Combined sources8
Helixi387 – 390Combined sources4
Helixi395 – 403Combined sources9
Beta strandi405 – 411Combined sources7
Helixi415 – 418Combined sources4
Helixi428 – 439Combined sources12
Beta strandi443 – 447Combined sources5
Beta strandi452 – 454Combined sources3
Helixi457 – 460Combined sources4
Helixi472 – 490Combined sources19
Turni491 – 493Combined sources3
Beta strandi496 – 501Combined sources6
Beta strandi508 – 510Combined sources3
Helixi513 – 515Combined sources3
Helixi519 – 523Combined sources5
Helixi534 – 546Combined sources13
Beta strandi551 – 558Combined sources8
Turni559 – 561Combined sources3
Helixi563 – 578Combined sources16
Beta strandi585 – 588Combined sources4
Beta strandi591 – 593Combined sources3
Helixi599 – 610Combined sources12
Turni611 – 613Combined sources3
Beta strandi615 – 631Combined sources17
Helixi638 – 659Combined sources22
Turni660 – 662Combined sources3
Beta strandi664 – 670Combined sources7
Helixi674 – 676Combined sources3
Helixi678 – 680Combined sources3
Beta strandi682 – 684Combined sources3
Beta strandi692 – 694Combined sources3
Helixi702 – 708Combined sources7
Helixi710 – 712Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4W8LX-ray1.76A/B/C367-718[»]
4XUNX-ray1.75A/B/C186-366[»]
4XUOX-ray1.70A/B29-186[»]
4XUPX-ray2.43A/B/C/D/E/F28-361[»]
4XUQX-ray1.95A/B/C186-366[»]
4XURX-ray1.67A/B/C186-366[»]
4XUTX-ray1.80A/B/C186-366[»]
ProteinModelPortaliO69230.
SMRiO69230.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 183CBM-cenC 1Add BLAST149
Domaini197 – 359CBM-cenC 2Add BLAST163
Domaini365 – 710GH10PROSITE-ProRule annotationAdd BLAST346

Domaini

Consists of three different domains. The central region of the enzyme is the catalytic domain. The N-terminal region contains cenC-type cellulose-binding domains and seems to act as a thermostabilizing domain: a derivative lacking this region shows a lower optimum temperature for activity (35 degrees Celsius) than the full-length enzyme, and a reduced thermal stability that results in a complete inactivation of the enzyme after 2 hours incubation at 55 degrees Celsius. The C-terminal region contains family 9 carbohydrate-binding modules.

Sequence similaritiesi

Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.1190. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR010502. Carb-bd_dom_fam9.
IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001000. GH10.
IPR031158. GH10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF06452. CBM9_1. 2 hits.
PF02018. CBM_4_9. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O69230-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGKWLRLCL AAVLIVSLLP GLGAGEWKAS AAKAGDILLS HSFEEGTTQG
60 70 80 90 100
WTARGGVKVD VTAEQAYQGK QSLQTTGRTE AWNGPSLSLT DVVHKNEVVE
110 120 130 140 150
ISGYVKLVAG SAPPDLKFTV ERRDRNGDTQ YDQVNAAEQV TDQKWVKLQG
160 170 180 190 200
QYSYEQGSSL LLYLESTDAK AAYLLDEFQI RLVKAAPENP GEPGEAGQAL
210 220 230 240 250
FKAYFEDGNI GNWRARGTEK LEVVSGIGHN SNRSLKTSSR SETYHGPLVE
260 270 280 290 300
VLPYLQKGST VHISFWAMYD EGPATQVING SLEKEFNRDT ANLEYAMFAS
310 320 330 340 350
TTLNKGQWKK IEADIIVPAE STGISGLRMY AETPWKQSSE VTETDTIPFY
360 370 380 390 400
VDDVQITATE AIAIEKNIPD LAKKLGSSYA LGAAIDQTAL DPKDPHSELL
410 420 430 440 450
TKHFNSITAG NFMKMDAMQP TEGKFVWSEA DKLVNFAAAN NMQVRGHTLL
460 470 480 490 500
WHSQVPDWFF TDPNDPSKPA TREQLMQRMK THIQTIVSRY KGKVHTWDVV
510 520 530 540 550
NEVISDGGGL RNQASGSKWR DIIGDVDGDG DDSDYIELAF RYAREADPDA
560 570 580 590 600
VLVINDYGIE GSVSKMNDMV KLVEKLLAKG TPIDAIGFQM HVSMYGPDIK
610 620 630 640 650
QIREAFNRAA ALGVHIQVTE LDMSIYSGNS EQEKPVTDEM MLEQAYRYRA
660 670 680 690 700
LFDLFKEFDD RGVMDSVTLW GLADDGTWLD DFPVKGRKDA PLLFDRKLKA
710 720 730 740 750
KPAYWALVDP STLPVYRNEW TASQAKVSLP DRKGQEDIIW GAVRALPFSH
760 770 780 790 800
VIEGAVGTTG EVKTLWDGKQ LNLRIEVKDA TRLKGDQVEV FVSPEDMTAG
810 820 830 840 850
KKNSTPKDGQ YIFNRDGGKG KDQKLYQVKE NKSGYVVYAS LPLSSADLAA
860 870 880 890 900
GKVLSLDFRI TDKQPNGKTS IVVWNDVNNQ QPQKTENRGK LKLGFDLKHA
910 920 930 940 950
KVMYGTPTVD GKEDKLWKKA VTITTDVKVT GNSGAKAKAK LLWDEKYLYV
960 970 980 990 1000
LAEVKDPLLS KKSANAHEQD SIELFIDLNK NQTNSYEEDD AQYRVNFDNE
1010 1020 1030 1040 1050
TSFGGSPRKE LFKSATRLTK EGYIVEAAIP LENVRTKESK WIGFDLQVND
1060 1070 1080
DGAGDGKRSS VFMWSDPSGN SYRDTSGFGS LLLMKK
Length:1,086
Mass (Da):120,586
Last modified:August 1, 1998 - v1
Checksum:i4378361F1801A326
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006645 Genomic DNA. Translation: CAA07173.1.
PIRiT17628.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006645 Genomic DNA. Translation: CAA07173.1.
PIRiT17628.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4W8LX-ray1.76A/B/C367-718[»]
4XUNX-ray1.75A/B/C186-366[»]
4XUOX-ray1.70A/B29-186[»]
4XUPX-ray2.43A/B/C/D/E/F28-361[»]
4XUQX-ray1.95A/B/C186-366[»]
4XURX-ray1.67A/B/C186-366[»]
4XUTX-ray1.80A/B/C186-366[»]
ProteinModelPortaliO69230.
SMRiO69230.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
CBM9. Carbohydrate-Binding Module Family 9.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.1190. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR010502. Carb-bd_dom_fam9.
IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001000. GH10.
IPR031158. GH10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF06452. CBM9_1. 2 hits.
PF02018. CBM_4_9. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYNC_PAEBA
AccessioniPrimary (citable) accession number: O69230
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 82 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.