Reviewed, UniProtKB/Swiss-Prot P29126 (XYNA_RUMFL)

Names and origin

Protein names

Recommended name:
    Bifunctional endo-1,4-beta-xylanase xylA
    EC=3.2.1.8

Gene names

Name:

xynA

Organism

Ruminococcus flavefaciens

Taxonomic identifier

1265 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Ruminococcaceae › Ruminococcus

Protein attributes

Sequence length	954 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	Xylanase domain 1 releases more xylo-oligosaccharides and domain 2 more xylose.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
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 10 (cellulase F) family.

Ontologies

Keywords
Biological process	Xylan degradation
Domain	Repeat 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	cation 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 – 27	27	Or 28, or 29 Potential
	Chain	28 – 954	927	Bifunctional endo-1,4-beta-xylanase xylA		PRO_0000008015
Regions
	Region	28 – 244	217	Xylanase domain 1
	Region	623 – 954	332	Xylanase domain 2
	Compositional bias	245 – 622	378	Asn/Gln/Trp-rich (linker)
Sites
	Active site	122	1	Nucleophile By similarity
	Active site	223	1	Proton donor By similarity
	Active site	774	1	Proton donor By similarity
	Active site	884	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	P29126-1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 1033567D4B526EBD	FASTA	954	111,362
	10 20 30 40 50 60 MKLSKIKKVL SGTVSALMIA SAAPVVASAA DQQTRGNVGG YDYEMWNQNG QGQASMNPGA 70 80 90 100 110 120 GSFTCSWSNI ENFLARMGKN YDSQKKNYKA FGNIVLTYDV EYTPRGNSYM CVYGWTRNPL 130 140 150 160 170 180 MEYYIVEGWG DWRPPGNDGE VKGTVSANGN TYDIRKTMRY NQPSLDGTAT FPQYWSVRQT 190 200 210 220 230 240 SGSANNQTNY MKGTIDVTKH FDAWSAAGLD MSGTLYEVSL NIEGYRSNGS ANVKSVSVTQ 250 260 270 280 290 300 GGSSDNGGQQ QNNDWNQQNN NQQQNNDWNN WGQQNNDWNQ WNNQGQQNND WNNWGQQNND 310 320 330 340 350 360 WNQWNNQGQQ QNNDWNNWGQ QNNDWNQWNN QGQQQNNDWN NWGQQNNDWN QWNNQGQQQN 370 380 390 400 410 420 NDWNNWGQQN NDWNQWNNQN NNQQNAWNGW DNNNNWNQNN QQQNNWDWNN QNNWNNNQQQ 430 440 450 460 470 480 NNDWNQWNNQ NNWNNNQQQN NDWNQWNNQG QQNNDWNQWN NQNNWNQNNN QQNAWNGWDN 490 500 510 520 530 540 NNNWNQWDQN NQWNNQQQNN TWDWNNQNNW NNNQQNNDWN QWNNQGQQQN NDWNQWNNQN 550 560 570 580 590 600 NNQNNGWDWN NQNNWNQNNN QQNAWNGWDN NNNWNQWGGQ NNDWNNQQQN NDWNQWNNQG 610 620 630 640 650 660 QQQNNDWNNQ NNWNQGQQNN NNSAGSSDSL KGAFSKYFKI GTSVSPHELN SGADFLKKHY 670 680 690 700 710 720 NSITPENELK PESILDQGAC QQKGNNVNTQ ISLSRAAQTL KFCEQNGIAL RGHTFVWYSQ 730 740 750 760 770 780 TPDWFFRENF SQNGAYVSKD IMNQRLESMI KNTFAALKSQ YPNLDVYSYD VCNELFLNNG 790 800 810 820 830 840 GGMRGADNSN WVKIYGDDSF VINAFKYARQ YAPAGCKLYL NDYNEYIPAK TNDIYNMAMK 850 860 870 880 890 900 LKQLGYIDGI GMQSHLATNY PDANTYETAL KKFLSTGLEV QITELDITCT NSAEQADLYE 910 920 930 940 950 KIFKLAMQNS AQIPAVTIWG TQDTVSWRSS QNPLLFSAGY QPKPAYDRVM ALAK

References

[1]

"A bifunctional xylanase encoded by the xynA gene of the rumen cellulolytic bacterium Ruminococcus flavefaciens 17 comprises two dissimilar domains linked by an asparagine/glutamine-rich sequence." Zhang J.-X., Flint H.J. Mol. Microbiol. 6:1013-1023(1992) [PubMed: 1584021] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 17.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z11127 Genomic DNA. Translation: CAA77476.1.
PIR	S20907.
3D structure databases
HSSP	HSSP built from PDB template 1F5J based on UniProtKB P77853.
ModBase	Search...
Protein family/group databases
CAZy	GH10. Glycoside Hydrolase Family 10. GH11. Glycoside Hydrolase Family 11.
Enzyme and pathway databases
BRENDA	3.2.1.8. 97801.
Family and domain databases
InterPro	IPR001000. Glyco_hydro_10. IPR001137. Glyco_hydro_11. IPR013319. Glyco_hydro_11/12_cat. IPR018208. Glyco_hydro_11_AS. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00331. Glyco_hydro_10. 1 hit. PF00457. Glyco_hydro_11. 1 hit. [Graphical view]
PRINTS	PR00911. GLHYDRLASE11.
SMART	SM00633. Glyco_10. 1 hit. [Graphical view]
PROSITE	PS00591. GLYCOSYL_HYDROL_F10. 1 hit. PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit. PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNA_RUMFL

Accession

Primary (citable) accession number: P29126

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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