Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endo-1,4-beta-xylanase C

Gene

xynC

Organism
Paenibacillus barcinonensis
Status
Reviewed-Annotation score: -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

Keywordsi

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

Enzyme and pathway databases

UniPathwayi
UPA00114

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

Proteomic databases

PRIDEiO69230

Structurei

Secondary structure

11086
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.120.260, 2 hits
InterProiView protein in InterPro
IPR010502 Carb-bd_dom_fam9
IPR003305 CenC_carb-bd
IPR008979 Galactose-bd-like_sf
IPR001000 GH10
IPR031158 GH10_AS
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF06452 CBM9_1, 2 hits
PF02018 CBM_4_9, 2 hits
PF00331 Glyco_hydro_10, 1 hit
PRINTSiPR00134 GLHYDRLASE10
SMARTiView protein in SMART
SM00633 Glyco_10, 1 hit
SUPFAMiSSF49785 SSF49785, 2 hits
SSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS00591 GH10_1, 1 hit
PS51760 GH10_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiXYNC_PAEBA
AccessioniPrimary (citable) accession number: O69230
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: August 1, 1998
Last modified: September 12, 2018
This is version 88 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again