Unreviewed, UniProtKB/TrEMBL Q7SI98 (Q7SI98_STROI)

Names and origin

Protein names	Submitted name:     Hydrolase PDB 1XYF PDB 1ISV PDB 1ISW PDB 1ISX PDB 1ISY PDB 1ISZ PDB 1IT0
Organism	Streptomyces olivaceoviridis (Streptomyces corchorusii) PDB 1XYF PDB 1ISV PDB 1ISW PDB 1ISX PDB 1ISY PDB 1ISZ PDB 1IT0
Taxonomic identifier	1921 [NCBI]
Taxonomic lineage	Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family. RuleBase RU003432V0

Ontologies

Keywords
Molecular function	Glycosidase RuleBase RU003432V0 Hydrolase
Technical term	3D-structure PDB 1XYF PDB 1ISV PDB 1ISW PDB 1ISX PDB 1ISY PDB 1ISZ PDB 1IT0
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q7SI98-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 6F26B9EC33801083	FASTA	436	46,749
	10 20 30 40 50 60 AESTLGAAAA QSGRYFGTAI ASGKLGDSAY TTIASREFNM VTAENEMKID ATEPQRGQFN 70 80 90 100 110 120 FSAGDRVYNW AVQNGKQVRG HTLAWHSQQP GWMQSLSGST LRQAMIDHIN GVMGHYKGKI 130 140 150 160 170 180 AQWDVVNEAF SDDGSGGRRD SNLQRTGNDW IEVAFRTARA ADPAAKLCYN DYNIENWTWA 190 200 210 220 230 240 KTQGVYNMVR DFKQRGVPID CVGFQSHFNS GSPYNSNFRT TLQNFAALGV DVAITELDIQ 250 260 270 280 290 300 GASSSTYAAV TNDCLAVSRC LGITVWGVRD TDSWRSGDTP LLFNGDGSKK AAYTAVLNAL 310 320 330 340 350 360 NGGSSTPPPS GGGQIKGVGS GRCLDVPNAS TTDGTQVQLY DCHSATNQQW TYTDAGELRV 370 380 390 400 410 420 YGDKCLDAAG TGNGTKVQIY SCWGGDNQKW RLNSDGSIVG VQSGLCLDAV GGGTANGTLI 430 QLYSCSNGSN QRWTRT

References

[1]	"An investigation of the nature and function of module 10 in a family F/10 xylanase FXYN of Streptomyces olivaceoviridis E-86 by module shuffling with the Cex of Cellulomonas fimi and by site-directed mutagenesis." Kaneko S., Kuno A., Fujimoto Z., Shimizu D., Machida S., Sato Y., Yura K., Go M., Mizuno H., Taira K., Kusakabe I., Hayashi K. FEBS Lett. 460:61-66(1999) [PubMed: 10571062] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[2]	"Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding module." Fujimoto Z., Kuno A., Kaneko S., Kobayashi H., Kusakabe I., Mizuno H. J. Mol. Biol. 316:65-78(2002) [PubMed: 11829503] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[3]	"Crystal structures of decorated xylooligosaccharides bound to a family 10 xylanase from Streptomyces olivaceoviridis E-86." Fujimoto Z., Kaneko S., Kuno A., Kobayashi H., Kusakabe I., Mizuno H. J. Biol. Chem. 279:9606-9614(2004) [PubMed: 14670957] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[4]	"Structure and function of a family 10 beta-xylanase chimera of Streptomyces olivaceoviridis E-86 FXYN and Cellulomonas fimi Cex." Kaneko S., Ichinose H., Fujimoto Z., Kuno A., Yura K., Go M., Mizuno H., Kusakabe I., Kobayashi H. J. Biol. Chem. 279:26619-26626(2004) [PubMed: 15078885] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-296.

Cross-references

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ISV	X-ray	2.10	A/B	1-436	[»]
1ISW	X-ray	2.10	A/B	1-436	[»]
1ISX	X-ray	2.10	A/B	1-436	[»]
1ISY	X-ray	2.10	A/B	1-436	[»]
1ISZ	X-ray	2.00	A/B	1-436	[»]
1IT0	X-ray	2.00	A/B	1-436	[»]
1V6U	X-ray	2.10	A/B	1-436	[»]
1V6V	X-ray	2.10	A/B	1-436	[»]
1V6W	X-ray	2.00	A/B	1-436	[»]
1V6X	X-ray	2.10	A/B	1-436	[»]
1V6Y	X-ray	2.20	A	1-239	[»]
1XYF	X-ray	1.90	A/B	1-436	[»]
2D1Z	X-ray	1.60	A/B	1-436	[»]
2D20	X-ray	1.85	A/B	1-436	[»]
2D22	X-ray	1.70	A/B	1-436	[»]
2D23	X-ray	1.95	A/B	1-436	[»]
2D24	X-ray	1.85	A/B	1-436	[»]
2G3I	X-ray	2.10	A	1-303	[»]
2G3J	X-ray	2.70	A	1-303	[»]
2G4F	X-ray	2.65	A/B	1-302	[»]

ModBase

Search...

Protein family/group databases

CAZy

CBM13. Carbohydrate-Binding Module Family 13.
GH10. Glycoside Hydrolase Family 10.

Family and domain databases

InterPro

IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_sg_catalytic.
IPR000772. Ricin_B_lectin.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF00331. Glyco_hydro_10. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]

PRINTS

PR00134. GLHYDRLASE10.

SMART

SM00633. Glyco_10. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]

PROSITE

PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

Q7SI98_STROI

Accession

Primary (citable) accession number: Q7SI98
Secondary accession number(s): Q7SID1

Entry history

Integrated into UniProtKB/TrEMBL:	December 15, 2003
Last sequence update:	December 15, 2003
Last modified:	June 16, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)