Carbohydrate-Binding Module Family 9

Known Activities	Modules of approx. 170 residues found so far only in xylanases. The cellulose-binding function has been demonstrated in one case.
3D Structure Status	b-sandwich
Note	Previously known as cellulose-binding domain family IX (CBD IX).
Statistics	GenBank accession (260); Uniprot accession (118); PDB accession (3); 3D entries (1); cryst (0)

Summary

All (296) Archaea (1) Bacteria (288) Eukaryota (1) unclassified (6) Structure (1 ) Characterized (39)


Bacteria
Protein Name	EC#	Organism	GenBank	Uniprot	PDB/3D
xylanase E (XynE)	3.2.1.8	Aeromonas caviae ME-1	BAA34091.1	Q9Z485
xylanase E (XynE)	3.2.1.8	Aeromonas caviae ME-1	BAA34091.1	Q9Z485
endo-β-1,4-xylanase (ORF2504) (Xyn10A)	3.2.1.8	Caldanaerobius polysaccharolyticus KMCJ	AFQ62797.1
endo-β-1,4-xylanase (ORF2504) (Xyn10A)	3.2.1.8	Caldanaerobius polysaccharolyticus KMCJ	AFQ62797.1
xylanase B (XynB)	3.2.1.8	Caldicellulosiruptor sp. Rt69B.1	AAB95325.1 CAA03086.1 CAE84530.1	O52373
xylanase B (XynB)	3.2.1.8	Caldicellulosiruptor sp. Rt69B.1	AAB95325.1	O52373
xylanase C (XynC;XylC)	3.2.1.8	Cellulomonas fimi ATCC 484	CAA90745.1	Q59278
xylanase C (XynC;XylC)	3.2.1.8	Cellulomonas fimi ATCC 484	CAA90745.1	Q59278
xylanase A (XynA) (Xyn10A)	3.2.1.8	Clostridium josui FERM P-9684	BAB20931.1	Q9F1V3
xylanase C / β-1,3-1,4-glucanase (XynC) (Xyn10B)	3.2.1.8	Clostridium stercorarium	BAA82143.1	Q9XDV5
celloxylanase (CelX;XynC) (Xyn10C)	3.2.1.8	Clostridium stercorarium NCIMB 11745	CAD48314.1	Q8GJ37
xylanase	3.2.1.8	Eubacterium ruminantium	BAA09971.1	Q47871
xylanase C (XynC;X-K)	3.2.1.8	Paenibacillus barcinonensis BP-23	CAA07173.1	O69230
xylanase C (XynC;X-K)	3.2.1.8	Paenibacillus barcinonensis BP-23	CAA07173.1	O69230
xylanase 10A (Xyn10A)	3.2.1.8	Paenibacillus curdlanolyticus B-6	ABZ80916.1	B1A3N2
methylglucuronoxylan xylanase A / xylanase A1 (XynA1;PbXynA1;XynA;Pjdr2_0221)	3.2.1.8	Paenibacillus sp. JDR-2	ACS98901.1 CAI79477.1	C6CRV0 Q53I45
xylanase 5 (Xyn5)	3.2.1.8	Paenibacillus sp. W-61	BAC45001.1	Q8GHJ4
xylanase A (XynA)	3.2.1.8	Thermoanaerobacterium saccharolyticum B6A-RI	AAA21812.1	P36917
xylanase A (XynA)	3.2.1.8	Thermoanaerobacterium saccharolyticum B6A-RI	AAA21812.1	P36917
endo-β-1,4-xylanase (XynA;XylA;Tsac_1459)	3.2.1.8	Thermoanaerobacterium saccharolyticum JW/SL-YS485	AAC43719.1 AFK86466.1	Q60043
endo-β-1,4-xylanase (XynA;XylA;Tsac_1459)	3.2.1.8	Thermoanaerobacterium saccharolyticum JW/SL-YS485	AAC43719.1 AFK86466.1	Q60043
xylanase X (XynX)	3.2.1.8	Thermoanaerobacterium sp.	AAA23227.1	P38535
xylanase X (XynX)	3.2.1.8	Thermoanaerobacterium sp.	AAA23227.1	P38535
xylanase (XynA) (salt-tolerant)	3.2.1.8	Thermoanaerobacterium sp. NTOU2	ADB23440.1
xylanase (XynA) (salt-tolerant)	3.2.1.8	Thermoanaerobacterium sp. NTOU2	ADB23440.1
xylanase A (XynA)	3.2.1.8	Thermoanaerobacterium thermosulfurigenes EM1	AAB08046.1	Q60046
xylanase A (XynA)	3.2.1.8	Thermoanaerobacterium thermosulfurigenes EM1	AAB08046.1	Q60046
xylanase A (XynA;Tm0061) (Xyl10A)	3.2.1.8	Thermotoga maritima MSB8	AAD35155.1 CAA86406.1 NP_227877.1	G4FGX6 Q60037	1I82[A] 1I8A[A] 1I8U[A]
xylanase A (XynA;Tm0061) (Xyl10A)	3.2.1.8	Thermotoga maritima MSB8	AAD35155.1 CAA86406.1 NP_227877.1	G4FGX6 Q60037
xylanase A (XynA;CTN_0632)	3.2.1.8	Thermotoga neapolitana DSM 4359	ACM22808.1 CAA87069.1	B9K775 Q60042
xylanase A (XynA;CTN_0632)	3.2.1.8	Thermotoga neapolitana DSM 4359	ACM22808.1 CAA87069.1	B9K775 Q60042
xylanase B (XynB)	3.2.1.8	Thermotoga sp. strain FjSS3-B.1	AAD32593.1 AAD32593.2	Q9R6T4
xylanase B (XynB)	3.2.1.8	Thermotoga sp. strain FjSS3-B.1	AAD32593.1 AAD32593.2	Q9R6T4
xylanase C (XynC)	3.2.1.8	Thermotoga sp. strain FjSS3-B.1	AAD32594.1	Q9WWJ9
xylanase C (XynC)	3.2.1.8	Thermotoga sp. strain FjSS3-B.1	AAD32594.1	Q9WWJ9
xylanase (Theth_1635) (Xyn10A)	3.2.1.8	Thermotoga thermarum DSM 5069	AEH51685.1
xylanase (Theth_1635) (Xyn10A)	3.2.1.8	Thermotoga thermarum DSM 5069	AEH51685.1
xylanase (Xyn10B)	3.2.1.8	Xylanimicrobium pachnodae	AAD54768.1	Q9RQB7
unclassified
Protein Name	EC#	Organism	GenBank	Uniprot	PDB/3D
xylanase A (Xyn-b39)	3.2.1.8	uncultured microorganism	AEI17090.1
Top

Footnotes

Experimental characterization exclusively covers enzyme activities at present. If you are aware of any missing experimental characterization that should be mentioned here, we encourage you to send your comment and support of the experimental evidence, including an electronic copy or appropriate link to the support material (i.e., article(s), thesis, database, etc), to cazy@afmb.univ-mrs.fr.