Unreviewed, UniProtKB/TrEMBL Q9RQB8 (Q9RQB8_9MICO)

Names and origin

Protein names

Recommended name:
    Endo-1,4-beta-xylanase RuleBase RU004392V0
    EC=3.2.1.8

Gene names

Name:

xyn11A EMBL AAD54767.1

Organism

Xylanimicrobium pachnodae EMBL AAD54767.1

Taxonomic identifier

101489 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Promicromonosporaceae › Xylanimicrobium

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. RuleBase RU004392V0
Pathway	Glycan degradation; xylan degradation. RuleBase RU004392V0
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family. RuleBase RU003433V0

Ontologies

Keywords
Biological process	Xylan degradation RuleBase RU003433V0
Molecular function	Glycosidase RuleBase RU003433V0 Hydrolase
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 polysaccharide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9RQB8-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 64EFDB808C25542D	FASTA	335	34,383
	10 20 30 40 50 60 MTRTISRAAH RPPAGGRIAR ALAAAGATVA MVIAGVAAAQ PAAAVDSNST GSSGGYFYSF 70 80 90 100 110 120 WTDAPGTVSM NLGSGGNYST SWSNTGNFVA GKGWSTGSAR TISYSGTFNP SGNAYLAVYG 130 140 150 160 170 180 WSHDPLVEYY IVDSWGTYRP TGTFMGTVNS DGGTYDIYKT TRTNAPSIEG TATFTQYWSV 190 200 210 220 230 240 RQSKRVGGTI TTANHFNAWA SHGMNLGRHD YQILATEGYQ SSGSSNITIG STSGGGGSGG 250 260 270 280 290 300 GTTTPPTNNG CTVQVTKGDE WGDRFNVSFT VSGSSSWKVA IALSGGQSLQ NSWSANVTGS 310 320 330 TGTLTATPNG SGNSFGITVY KNGSSTLPTA TCSTT

References

[1]	"Molecular and biochemical characterization of two xylanase-encoding genes from Cellulomonas pachnodae." Cazemier A.E., Verdoes J.C., van Ooyen A.J., Op den Camp H.J. Appl. Environ. Microbiol. 65:4099-4107(1999) [PubMed: 10473422] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF120156 Genomic DNA. Translation: AAD54767.1.
3D structure databases
HSSP	HSSP built from PDB template 1M4W based on UniProtKB Q8GMV7.
SMR	Q9RQB8. Positions 45-220.
ModBase	Search...
Protein family/group databases
CAZy	CBM2. Carbohydrate-Binding Module Family 2. GH11. Glycoside Hydrolase Family 11.
Family and domain databases
InterPro	IPR001919. CBD_bac. IPR012291. CBD_carb_bd. IPR001137. Glyco_hydro_11. IPR013319. Glyco_hydro_11/12_cat. IPR018208. Glyco_hydro_11_AS. [Graphical view]
Gene3D	G3DSA:2.60.40.290. CBD_carb_bd. 1 hit. G3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.
Pfam	PF00553. CBM_2. 1 hit. PF00457. Glyco_hydro_11. 1 hit. [Graphical view]
PRINTS	PR00911. GLHYDRLASE11.
SMART	SM00637. CBD_II. 1 hit. [Graphical view]
PROSITE	PS51173. CBM2. 1 hit. PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit. PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q9RQB8_9MICO

Accession

Primary (citable) accession number: Q9RQB8

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2000
Last sequence update:	May 1, 2000
Last modified:	May 5, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)