Q12667 (XYNA_PIRSP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endo-1,4-beta-xylanase A
EC=3.2.1.8

Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
Xylanase A
Short name=XYLA

Gene names

Name:

XYNA

Organism

Piromyces sp.

Taxonomic identifier

45796 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Neocallimastigomycota › Neocallimastigomycetes › Neocallimastigales › Neocallimastigaceae › Piromyces

Protein attributes

Sequence length	625 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Hydrolyzes 1,4-beta linked polysaccharide backbones of xylans, one of the major hemicellulose components in hardwoods and softwoods. It is more active against xylopentaose than xylotetraose, has trace activity against xylotriose. The major products released from hydrolysis of xylooligosaccharides are xylobiose and xylotriose. The reiterated 40 AA domain is involved in binding the cellulase-hemicellulase complex.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Domain	Consists of an N- and C-terminal catalytic domains linked to a middle reiterated domain. Only the C-terminal catalytic domain is active.
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family.

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	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 – 19	19	Potential
	Chain	20 – 625	606	Endo-1,4-beta-xylanase A		PRO_0000008017
Regions
	Repeat	259 – 268	10	1-1
	Repeat	269 – 278	10	1-2
	Repeat	284 – 325	42	2-1
	Repeat	331 – 372	42	2-2
	Region	20 – 254	235	Catalytic 1
	Region	255 – 279	25	Linker
	Region	259 – 278	20	2 X 10 AA tandem repeats of G-Q-G-[LQ]-G-N-G-Q-G-[NQ]
	Region	284 – 372	89	2 X 42 AA approximate repeats
	Region	374 – 403	30	Linker
	Region	404 – 625	222	Catalytic 2
Sites
	Active site	510	1	Nucleophile By similarity
	Active site	603	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q12667 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 9DA99B6A17290922	FASTA	625	68,049
	10 20 30 40 50 60 MKLFQIFPLL LSLTSVTLAA DDFCNATGFQ GQSVVSTGHD VKKIGNIDYE QWADGGNNSA 70 80 90 100 110 120 TFYSDGSFKC NFSNTKDYLC RSGVAFSQAK YPSEIGHIEA EYRLVKKSAS NVGYSYVGVY 130 140 150 160 170 180 GWTLQSGISG VYEYYIVDNW LSQWRPGDWV GNTKFGDFTI DGGVYTVYKN VNGNLTQYFS 190 200 210 220 230 240 LRKSERTCGT IDVTAHFAQW EKLGLKMPKI TEIKVLAEAG NTGGGCSGSV EIPYAKIYIN 250 260 270 280 290 300 GKDQDGKSKG GSSSGGSNGQ GLGNGQGNGQ GQGNGQGQSA TGSGKCPSTI TSQGYKCCSS 310 320 330 340 350 360 NCDIIYRDQS GDWGVENDEW CGCGSRVPKT TNCPSSIKNQ GYKCCSDSCE IVLTDSDGDW 370 380 390 400 410 420 GIENDEWCGC GIKNTTPTTT TKKSNNSQPT QGQSNNNSST NTNFCSTSKH SGQSVTETSN 430 440 450 460 470 480 KVGSIGGVGY ELWADSGNNS ATFYSDGSFS CSFRNAKDYL CRSGLSFDST KTYQQLGHMY 490 500 510 520 530 540 ADFKLVKQNI QNVDYSYVGI YGWTRNPLVE FYVVDNWLSQ WRPGDWVGNK KHGDFTIDGA 550 560 570 580 590 600 KYTVYENTRT GPSIDGNTTF KQYFSIRQQA RDCGTIDITA HFEQWEKLGM RMGKMHEAKV 610 620 LGEAGSTGSG TSGTADFPYA KVYIK

References

[1]

"The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain." Fanutti C., Ponyi T., Black G.W., Hazlewood G.P., Gilbert H.J. J. Biol. Chem. 270:29314-29322(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X91858 mRNA. Translation: CAA62969.1.
3D structure databases
ProteinModelPortal	Q12667.
SMR	Q12667. Positions 292-323.
ModBase	Search...
Protein family/group databases
CAZy	GH11. Glycoside Hydrolase Family 11.
mycoCLAP	XYN11A_PIRSP.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00114.
Family and domain databases
Gene3D	2.60.120.180. 2 hits. 3.90.1220.10. 2 hits.
InterPro	IPR002883. CBM10/Dockerin_dom. IPR008985. ConA-like_lec_gl_sf. IPR009034. Dockerin_dom. IPR001137. Glyco_hydro_11. IPR013319. Glyco_hydro_11/12. IPR018208. Glyco_hydro_11_AS. [Graphical view]
Pfam	PF02013. CBM_10. 2 hits. PF00457. Glyco_hydro_11. 2 hits. [Graphical view]
PRINTS	PR00911. GLHYDRLASE11.
SUPFAM	SSF49899. ConA_like_lec_gl. 2 hits. SSF64571. Dockering_CDD. 2 hits.
PROSITE	PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit. PS00777. GLYCOSYL_HYDROL_F11_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNA_PIRSP

Accession

Primary (citable) accession number: Q12667

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program