Q59675 (Q59675_9GAMM) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Submitted name: Endo-beta-1,4-xylanase EMBL CAA88764.2 EC=3.2.1.8 EMBL CAA88764.2
Organism	Cellvibrio japonicus EMBL CAA88764.2
Taxonomic identifier	155077 [NCBI]
Taxonomic lineage	Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Cellvibrio

Protein attributes

Sequence length	606 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family. RuleBase RU003432

Ontologies

Keywords
Biological process	Xylan degradation EMBL CAA88764.2
Domain	Signal EMBL CAA88764.2
Molecular function	Glycosidase RuleBase RU003432 EMBL CAA88764.2 Hydrolase
Technical term	3D-structure PDB 1US3 PDB 1GNY PDB 1US2
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 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 EMBL CAA88764.2
	Chain	20 – 606	587	Potential EMBL CAA88764.2		PRO_5000147609

Sequences

	Sequence		Length	Mass (Da)
	Q59675 [UniParc]. Last modified March 1, 2004. Version 2. Checksum: 56E149954CE6BFEE	FASTA	606	64,884
	10 20 30 40 50 60 MKKIQQLLML SLISSTLIAC GGGGGGGSTP TTSSSPQSSS PASTPSSASS SSIISSSSLS 70 80 90 100 110 120 SSLSSSSLSS SSLSSSSASS VSSSSVAASE GNVVIEVDMA NGWRGNASGS TSHSGITYSA 130 140 150 160 170 180 DGVTFAALGD GVGAVFDIAR PTTLEDAVIA MVVNVSAEFK ASEANLQIFA QLKEDWSKGE 190 200 210 220 230 240 WDCLAASSEL TADTDLTLTC TIDEDDDKFN QTARDVQVGI QAKGTPAGTI TIKSVTITLA 250 260 270 280 290 300 QEAYSANVDH LRDLAPSDFP IGVAVSNTDS ATYNLLTNSR EQAVVKKHFN HLTAGNIMKM 310 320 330 340 350 360 SYMQPTEGNF NFTNADAFVD WATENNMTVH GHALVWHSDY QVPNFMKNWA GSAEDFLAAL 370 380 390 400 410 420 DTHITTIVDH YEAKGNLVSW DVVNEAIDDN SPANFRTTDS AFYVKSGNSS VYIERAFQTA 430 440 450 460 470 480 RAADPAVILY YNDYNIEQNN AKTTKMVDMV KDFQARSIPI DGVGFQMHVC MNYPSIANIS 490 500 510 520 530 540 AAMKKVVDLG LLVKITELDV AVNQPHCDAY PANKINPLTE AAQLAQKKRY CDVVKAYLDT 550 560 570 580 590 600 VPVNQRGGIS VWGTTDANTW LDGLYREQFE DEKISWPLLF DNNYNDKPAL RGFADALIGT QCTNTH

References

[1]	"Novel cellulose-binding domains, NodB homologues and conserved modular architecture in xylanases from the aerobic soil bacteria Pseudomonas fluorescens subsp. cellulosa and Cellvibrio mixtus." Millward-Sadler S.J., Davidson K., Hazlewood G.P., Black G.W., Gilbert H.J., Clarke J.H. Biochem. J. 312:39-48(1995) [PubMed: 7492333] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	Gilbert H.J. Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Structure of a family 15 carbohydrate-binding module in complex with xylopentaose. Evidence that xylan binds in an approximate 3-fold helical conformation." Szabo L., Jamal S., Xie H., Charnock S.J., Bolam D.N., Gilbert H.J., Davies G.J. J. Biol. Chem. 276:49061-49065(2001) [PubMed: 11598143] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 91-243.
[4]	"Structural and biochemical analysis of Cellvibrio japonicus xylanase 10C: how variation in substrate-binding cleft influences the catalytic profile of family GH-10 xylanases." Pell G., Szabo L., Charnock S.J., Xie H., Gloster T.M., Davies G.J., Gilbert H.J. J. Biol. Chem. 279:11777-11788(2004) [PubMed: 14670951] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 86-606.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z48928 Genomic DNA. Translation: CAA88764.2.

PIR

S59634.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GNY	X-ray	1.63	A	91-243	[»]
1US2	X-ray	1.85	A	86-606	[»]
1US3	X-ray	1.85	A	86-606	[»]

ProteinModelPortal

Q59675.

SMR

Q59675. Positions 95-606.

ModBase

Search...

Protein family/group databases

CAZy

CBM15. Carbohydrate-Binding Module Family 15.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR005088. CBM_fam15.
IPR008979. Galactose-bd-like.
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

PF03426. CBM_15. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]

PRINTS

PR00134. GLHYDRLASE10.

SMART

SM00633. Glyco_10. 1 hit.
[Graphical view]

SUPFAM

SSF49785. Gal_bind_like. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q59675_9GAMM

Accession

Primary (citable) accession number: Q59675

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	March 1, 2004
Last modified:	May 31, 2011
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)