Reviewed, UniProtKB/Swiss-Prot P23552 (XYNB_CALSA)

Names and origin

Protein names

Recommended name:
    Beta-xylosidase
    EC=3.2.1.37
Alternative name(s):
    1,4-beta-D-xylan xylohydrolase
    Xylan 1,4-beta-xylosidase

Gene names

Name:

xynB

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

General annotation (Comments)

Function	Beta-xylosidase is an intracellular xylan-degrading enzyme.
Catalytic activity	Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.
Sequence similarities	Belongs to the glycosyl hydrolase 39 family.
Caution	It is uncertain whether Met-1 or Met-7 is the initiator.

Ontologies

Keywords
Biological process	Xylan degradation
Molecular function	Glycosidase Hydrolase
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 xylan 1,4-beta-xylosidase 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 – 488	488	Beta-xylosidase		PRO_0000057688
Sites
	Active site	163	1	Proton donor Potential
	Active site	275	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	P23552-1 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 7B8801B1B26F4640	FASTA	488	56,366
	10 20 30 40 50 60 MERRKIMKIT INYGKRLGKI NKFWAKCVGS CHATTALRED WRKQLKKCRD ELGFEYIRFH 70 80 90 100 110 120 GWLNDDMSVC FRNDDGLLSF SFFNIDSIID FLLEIGMKPF IELSFMPEAL ASGTKTVFHY 130 140 150 160 170 180 KGNITPPKSY EEWGQLIEEL ARHLISRYGK NEVREWFFEV WNEPNLKDFF WAGTMEEYFK 190 200 210 220 230 240 LYKYAAFAIK KVDSELRVGG PATAIDAWIP ELKDFCTKNG VPIDFISTHQ YPTDLAFSTS 250 260 270 280 290 300 SNMEEAMAKA KRGELAERVK KALEEAYPLP VYYTEWNNSP SPRDPYHDIP YDAAFIVKTI 310 320 330 340 350 360 IDIIDLPLGC YSYWTFTDIF EECGQSSLPF HGGFGLLNIH GIPKPSYRAF QILDKLNGER 370 380 390 400 410 420 IEIEFEDKSP TIDCIAVQNE REIILVISNH NVPLSPIDTE NIKVVLKGIE NCREVFVERI 430 440 450 460 470 480 DEYNANPKRV WLEMGSPAYL NREQIEELIK ASELKKEKVS WGIVNNNEIT FDLSVLPHSV VAVTIKNG

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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M34459 Genomic DNA. Translation: AAA23063.1. AF005383 Genomic DNA. Translation: AAB87376.1.
PIR	T30914.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH39. Glycoside Hydrolase Family 39.
Enzyme and pathway databases
BRENDA	3.2.1.37. 15230.
Family and domain databases
InterPro	IPR000514. Glyco_hydro_39. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF01229. Glyco_hydro_39. 1 hit. [Graphical view]
PRINTS	PR00745. GLHYDRLASE39.
PROSITE	PS01027. GLYCOSYL_HYDROL_F39. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNB_CALSA

Accession

Primary (citable) accession number: P23552

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	June 16, 2009
This is version 55 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)