O69230 (XYNC_PAEBA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endo-1,4-beta-xylanase C
Short name=Xylanase C
EC=3.2.1.8

Alternative name(s):
1,4-beta-D-xylan xylanohydrolase C

Gene names

Name:

xynC

Organism

Paenibacillus barcinonensis

Taxonomic identifier

198119 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Paenibacillaceae › Paenibacillus

Protein attributes

Sequence length	1086 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Ref.1
Pathway	Glycan degradation; xylan degradation.
Domain	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 similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family. Contains 2 CBM-cenC (cenC-type cellulose-binding) domains.
Biophysicochemical properties	pH dependence: 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. Ref.1 Temperature dependence: 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.

Ontologies

Keywords
Biological process	Xylan degradation
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Potential
	Chain	32 – 1086	1055	Endo-1,4-beta-xylanase C		PRO_0000371420
Regions
	Domain	35 – 183	149	CBM-cenC 1
	Domain	197 – 359	163	CBM-cenC 2
	Region	370 – 711	342	Catalytic
Sites
	Active site	502	1	Proton donor By similarity
	Active site	556	1	By similarity
	Active site	620	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	O69230 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 4378361F1801A326	FASTA	1,086	120,586
	10 20 30 40 50 60 MRGKWLRLCL AAVLIVSLLP GLGAGEWKAS AAKAGDILLS HSFEEGTTQG WTARGGVKVD 70 80 90 100 110 120 VTAEQAYQGK QSLQTTGRTE AWNGPSLSLT DVVHKNEVVE ISGYVKLVAG SAPPDLKFTV 130 140 150 160 170 180 ERRDRNGDTQ YDQVNAAEQV TDQKWVKLQG QYSYEQGSSL LLYLESTDAK AAYLLDEFQI 190 200 210 220 230 240 RLVKAAPENP GEPGEAGQAL FKAYFEDGNI GNWRARGTEK LEVVSGIGHN SNRSLKTSSR 250 260 270 280 290 300 SETYHGPLVE VLPYLQKGST VHISFWAMYD EGPATQVING SLEKEFNRDT ANLEYAMFAS 310 320 330 340 350 360 TTLNKGQWKK IEADIIVPAE STGISGLRMY AETPWKQSSE VTETDTIPFY VDDVQITATE 370 380 390 400 410 420 AIAIEKNIPD LAKKLGSSYA LGAAIDQTAL DPKDPHSELL TKHFNSITAG NFMKMDAMQP 430 440 450 460 470 480 TEGKFVWSEA DKLVNFAAAN NMQVRGHTLL WHSQVPDWFF TDPNDPSKPA TREQLMQRMK 490 500 510 520 530 540 THIQTIVSRY KGKVHTWDVV NEVISDGGGL RNQASGSKWR DIIGDVDGDG DDSDYIELAF 550 560 570 580 590 600 RYAREADPDA VLVINDYGIE GSVSKMNDMV KLVEKLLAKG TPIDAIGFQM HVSMYGPDIK 610 620 630 640 650 660 QIREAFNRAA ALGVHIQVTE LDMSIYSGNS EQEKPVTDEM MLEQAYRYRA LFDLFKEFDD 670 680 690 700 710 720 RGVMDSVTLW GLADDGTWLD DFPVKGRKDA PLLFDRKLKA KPAYWALVDP STLPVYRNEW 730 740 750 760 770 780 TASQAKVSLP DRKGQEDIIW GAVRALPFSH VIEGAVGTTG EVKTLWDGKQ LNLRIEVKDA 790 800 810 820 830 840 TRLKGDQVEV FVSPEDMTAG KKNSTPKDGQ YIFNRDGGKG KDQKLYQVKE NKSGYVVYAS 850 860 870 880 890 900 LPLSSADLAA GKVLSLDFRI TDKQPNGKTS IVVWNDVNNQ QPQKTENRGK LKLGFDLKHA 910 920 930 940 950 960 KVMYGTPTVD GKEDKLWKKA VTITTDVKVT GNSGAKAKAK LLWDEKYLYV LAEVKDPLLS 970 980 990 1000 1010 1020 KKSANAHEQD SIELFIDLNK NQTNSYEEDD AQYRVNFDNE TSFGGSPRKE LFKSATRLTK 1030 1040 1050 1060 1070 1080 EGYIVEAAIP LENVRTKESK WIGFDLQVND DGAGDGKRSS VFMWSDPSGN SYRDTSGFGS LLLMKK

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ006645 Genomic DNA. Translation: CAA07173.1.
PIR	T17628.
3D structure databases
HSSP	HSSP built from PDB template 1I8A based on UniProtKB Q60037.
ProteinModelPortal	O69230.
ModBase	Search...
Protein family/group databases
CAZy	CBM22. Carbohydrate-Binding Module Family 22. CBM9. Carbohydrate-Binding Module Family 9. GH10. Glycoside Hydrolase Family 10.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00114.
Family and domain databases
Gene3D	2.60.40.1190. 2 hits. 3.20.20.80. 1 hit.
InterPro	IPR010502. Carb-bd_dom_fam9. IPR008960. Carb-bd_dom_fam9-like. IPR015922. Carb-bd_dom_fam9-like_subgr. IPR003305. CenC_carb-bd. IPR008979. Galactose-bd-like. IPR001000. Glyco_hydro_10. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF02018. CBM_4_9. 2 hits. PF06452. DUF1083. 2 hits. PF00331. Glyco_hydro_10. 1 hit. [Graphical view]
PRINTS	PR00134. GLHYDRLASE10.
SMART	SM00633. Glyco_10. 1 hit. [Graphical view]
SUPFAM	SSF49344. CBD9-like. 2 hits. SSF49785. Gal_bind_like. 2 hits. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00591. GLYCOSYL_HYDROL_F10. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNC_PAEBA

Accession

Primary (citable) accession number: O69230

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program