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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei502 – 5021Proton donorBy similarity
Active sitei556 – 5561By similarity
Active sitei620 – 6201NucleophilePROSITE-ProRule annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence analysisAdd
BLAST
Chaini32 – 10861055Endo-1,4-beta-xylanase CPRO_0000371420Add
BLAST

Structurei

Secondary structure

1
1086
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 415Combined sources
Beta strandi45 – 473Combined sources
Beta strandi52 – 565Combined sources
Beta strandi58 – 647Combined sources
Beta strandi67 – 704Combined sources
Beta strandi72 – 765Combined sources
Beta strandi84 – 885Combined sources
Turni90 – 923Combined sources
Beta strandi98 – 10710Combined sources
Beta strandi114 – 12310Combined sources
Beta strandi129 – 1335Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi146 – 1527Combined sources
Beta strandi158 – 16811Combined sources
Beta strandi173 – 18412Combined sources
Beta strandi201 – 2033Combined sources
Beta strandi216 – 2183Combined sources
Beta strandi220 – 2267Combined sources
Beta strandi229 – 23810Combined sources
Beta strandi248 – 2503Combined sources
Helixi252 – 2543Combined sources
Beta strandi260 – 2689Combined sources
Beta strandi271 – 28616Combined sources
Beta strandi294 – 30411Combined sources
Beta strandi309 – 3168Combined sources
Helixi320 – 3223Combined sources
Beta strandi324 – 3329Combined sources
Helixi338 – 3403Combined sources
Helixi344 – 3463Combined sources
Beta strandi349 – 35810Combined sources
Helixi371 – 3755Combined sources
Beta strandi378 – 3858Combined sources
Helixi387 – 3904Combined sources
Helixi395 – 4039Combined sources
Beta strandi405 – 4117Combined sources
Helixi415 – 4184Combined sources
Helixi428 – 43912Combined sources
Beta strandi443 – 4475Combined sources
Beta strandi452 – 4543Combined sources
Helixi457 – 4604Combined sources
Helixi472 – 49019Combined sources
Turni491 – 4933Combined sources
Beta strandi496 – 5016Combined sources
Beta strandi508 – 5103Combined sources
Helixi513 – 5153Combined sources
Helixi519 – 5235Combined sources
Helixi534 – 54613Combined sources
Beta strandi551 – 5588Combined sources
Turni559 – 5613Combined sources
Helixi563 – 57816Combined sources
Beta strandi585 – 5884Combined sources
Beta strandi591 – 5933Combined sources
Helixi599 – 61012Combined sources
Turni611 – 6133Combined sources
Beta strandi615 – 63117Combined sources
Helixi638 – 65922Combined sources
Turni660 – 6623Combined sources
Beta strandi664 – 6707Combined sources
Helixi674 – 6763Combined sources
Helixi678 – 6803Combined sources
Beta strandi682 – 6843Combined sources
Beta strandi692 – 6943Combined sources
Helixi702 – 7087Combined sources
Helixi710 – 7123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 183149CBM-cenC 1Add
BLAST
Domaini197 – 359163CBM-cenC 2Add
BLAST
Domaini365 – 710346GH10PROSITE-ProRule annotationAdd
BLAST

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
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.
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...

Publicationsi

  1. "A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes."
    Blanco A., Diaz P., Zueco J., Parascandola P., Pastor F.I.J.
    Microbiology 145:2163-2170(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: DSM 15478 / CECT 7022 / BP-23.

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: March 16, 2016
This is version 80 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.