Reviewed, UniProtKB/Swiss-Prot Q53317 (XYND_RUMFL)

Names and origin

Protein names

Recommended name:
    Xylanase/beta-glucanase
Including the following 2 domains:
    1- Recommended name:
            Endo-1,4-beta-xylanase
                Short name=Xylanase
              EC=3.2.1.8
    2- Recommended name:
            Endo-beta-1,3-1,4 glucanase
              EC=3.2.1.73
        Alternative name(s):
            1,3-1,4-beta-D-glucan 4-glucanohydrolase
            Lichenase

Gene names

Name:

xynD

Organism

Ruminococcus flavefaciens

Taxonomic identifier

1265 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Ruminococcaceae › Ruminococcus

Protein attributes

Sequence length	802 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Contains two catalytic domains with xylanase and endo-beta-1,3-1,4 glucanase activities.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.
Pathway	Glycan degradation; xylan degradation.
Sequence similarities	In the N-terminal section; belongs to the glycosyl hydrolase 11 (cellulase G) family. In the C-terminal section; belongs to the glycosyl hydrolase 16 family. Contains 1 CBM-cenC (cenC-type cellulose-binding) domain.

Ontologies

Keywords
Biological process	Xylan degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC licheninase 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 – 802	771	Xylanase/beta-glucanase		PRO_0000008009
Regions
	Domain	258 – 404	147	CBM-cenC
	Region	32 – 244	213	A (xylanase)
	Region	245 – 523	279	B
	Region	524 – 555	32	Linker
	Region	556 – 802	247	C (beta-glucanase)
	Compositional bias	524 – 529	6	Poly-Thr
	Compositional bias	532 – 543	12	Poly-Thr
	Compositional bias	546 – 553	8	Poly-Thr
Sites
	Active site	124	1	Nucleophile By similarity
	Active site	226	1	Proton donor By similarity
	Active site	684	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q53317-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 2880A689647284AF	FASTA	802	89,091
	10 20 30 40 50 60 MKKSIFKRYA AAVGLMASVL MFTAVPTTSN AADDQKTGKV GGFDWEMWNQ NYTGTVSMNP 70 80 90 100 110 120 GAGSFTCSWS GIENFLARMG KNYDDQKKNY KAFGDIVLTY DVEYTPRGNS YMCIYGWTRN 130 140 150 160 170 180 PLMEYYIVEG WGDWEPPGND GVDNFGTTTI DGKTYKIRKS MRYNQPSIEG TKTFPQYWSV 190 200 210 220 230 240 RTTSGSRNNT TNYMKDQVSV TKHFDAWSKA GLDMSGTLYE VSLNIEGYRS NGSANVKSIS 250 260 270 280 290 300 FDGGIDIPDP EPIKPDENGY YLKENFESGE GNWSGRGSAK VKSSSGYDGT KGIFVSGRED 310 320 330 340 350 360 TWNGASINLD ELTFKAGETY SLGTAVMQDF ESSVDFKLTL QYTDADGKEN YDEVKTVTAA 370 380 390 400 410 420 KGQWVDLSNS SYTIPSGATG LVLYVEVPES KTDFYMDGAY AGVKGTKPLI SISSQSVDPP 430 440 450 460 470 480 VTEPTNPTNP TGPSVTKWGD ANCDGGVDLS DAIFIMQFLA NPNKYGLTGT ETNHMTNQGK 490 500 510 520 530 540 VNGDVCEHGS GLTEDDAVSI QKYLIRAISE LPESYLEGHD PSKTTTTTTR ITTTTTTTTT 550 560 570 580 590 600 TTTSKTTTTT TTTSPAMHGG YRDLGTPMNT SATMISDFRT GKAGDFFASD GWTNGKPFDC 610 620 630 640 650 660 WWYKRNAVIN DGCLQLSIDQ KWTNDKNPDW DPRYSGGEFR TNNFYHYGYY ECSMQAMKND 670 680 690 700 710 720 GVVSSFFTYT GPSDDNPWDE IDIEILGKNT TQVQFNYYTN GQGKHEKLYD LGFDSSEAYH 730 740 750 760 770 780 TYGFDWQPNY IAWYVDGREV YRATQDIPKT PGKIMMNAWP GLTVDDWLKA FNGRTPLTAH 790 800 YQWVTYNKNG VQHSSQGQNP WG

References

[1]

"A bifunctional enzyme, with separate xylanase and beta(1,3-1,4)-glucanase domains, encoded by the xynD gene of Ruminococcus flavefaciens." Flint H.J., Martin J., McPherson C.A., Daniel A.S., Zhang J.-X. J. Bacteriol. 175:2943-2951(1993) [PubMed: 8491715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 17.

Cross-references

Sequence databases
EMBLGenBankDDBJ	S61204 Genomic DNA. Translation: AAB26620.1.
3D structure databases
HSSP	HSSP built from PDB template 1AJK based on UniProtKB P23904.
ModBase	Search...
Protein family/group databases
CAZy	CBM22. Carbohydrate-Binding Module Family 22. GH11. Glycoside Hydrolase Family 11. GH16. Glycoside Hydrolase Family 16.
Enzyme and pathway databases
BRENDA	3.2.1.73. 97801. 3.2.1.8. 97801.
Family and domain databases
InterPro	IPR008264. Beta_glucanase. IPR003305. CenC_carb_bd. IPR013320. ConA-like_subgrp. IPR001137. Glyco_hydro_11. IPR013319. Glyco_hydro_11/12_cat. IPR018208. Glyco_hydro_11_AS. IPR000757. Glyco_hydro_16. IPR008263. Glycoside_hydrolase_16_AS. [Graphical view]
Gene3D	G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit. G3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.
Pfam	PF02018. CBM_4_9. 1 hit. PF00457. Glyco_hydro_11. 1 hit. PF00722. Glyco_hydro_16. 1 hit. [Graphical view]
PRINTS	PR00737. GLHYDRLASE16.
PROSITE	PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit. PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit. PS01034. GLYCOSYL_HYDROL_F16. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYND_RUMFL

Accession

Primary (citable) accession number: Q53317

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)