P23556 (XYNA_CALSA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A

Gene names

Name:

xynA

Organism

Caldocellum saccharolyticum (Caldicellulosiruptor saccharolyticus)

Taxonomic identifier

44001 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Caldicellulosiruptor

Protein attributes

Sequence length	342 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family. Cytoplasmic xylanase subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 5.5-6.0. Temperature dependence: Optimum temperature is 70 degrees Celsius.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Cytoplasm
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Chain	1 – 342	342	Endo-1,4-beta-xylanase A		PRO_0000007984
Sites
	Active site	144	1	Proton donor By similarity
	Active site	252	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	P23556 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: C5380F2AB0CC0271	FASTA	342	40,455
	10 20 30 40 50 60 MRCLIVCENL EMLNLSLAKT YKDYFKIGAA VTAKDLEGVH RDILLKHFNS LTPENAMKFE 70 80 90 100 110 120 NIHPEEQRYN FEEVARIKEF AIKNDMKLRG HTFVWHNQTP GWVFLDKNGE EASKELVIER 130 140 150 160 170 180 LREHIKTLCE RYKDVVYAWD VVNEAVEDKT EKLLRESNWR KIIGDDYIKI AFEIAREYAG 190 200 210 220 230 240 DAKLFYNDYN NEMPYKLEKT YKVLKELLER GTPIDGIGIQ AHWNIWDKNL VSNLKKAIEV 250 260 270 280 290 300 YASLGLEIHI TELDISVFEF EDKRTDLFEP TPEMLELQAK VYEDVFAVFR EYKDVITSVT 310 320 330 340 LWGISDRHTW KDNFPVKGRK DWPLLFDVNG KPKEALYRIL RF

References

[1]	"Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile 'Caldocellum saccharolyticum'." Luethi E., Love D.R., McAnulty J., Wallace C., Caughey P.A., Saul D.J., Bergquist P.L. Appl. Environ. Microbiol. 56:1017-1024(1990) [PubMed: 2111111] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A cluster of genes involved in xylan degradation cloned from the extreme thermophile Caldicellulosiruptor saccharolyticus." Te'O V.S. Jr., Gibbs M.D., Saul D.J., Bergquist P.L. Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Xylanase from the extremely thermophilic bacterium 'Caldocellum saccharolyticum': overexpression of the gene in Escherichia coli and characterization of the gene product." Luethi E., Jasmat N.B., Bergquist P.L. Appl. Environ. Microbiol. 56:2677-2683(1990) [PubMed: 2275529] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M34459 Genomic DNA. Translation: AAA23059.1. AF005383 Genomic DNA. Translation: AAB87374.1.
PIR	A60154. A37202.
3D structure databases
ProteinModelPortal	P23556.
SMR	P23556. Positions 16-341.
ModBase	Search...
Protein family/group databases
CAZy	GH10. Glycoside Hydrolase Family 10.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001000. Glyco_hydro_10. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00331. Glyco_hydro_10. 1 hit. [Graphical view]
PRINTS	PR00134. GLHYDRLASE10.
SMART	SM00633. Glyco_10. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00591. GLYCOSYL_HYDROL_F10. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNA_CALSA

Accession

Primary (citable) accession number: P23556

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	May 31, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program