O87119 (O87119_CLOTM) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Xylanase EMBL BAA33543.1

Gene names

Name:

xynA EMBL BAA33543.1

Organism

Clostridium thermocellum EMBL BAA33543.1

Taxonomic identifier

1515 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	683 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Biological process	Xylan degradation EMBL BAA33543.1
Technical term	3D-structure PDB 2C79 PDB 2C71
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: InterPro xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds 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)
	O87119 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: C5F39D05C2145ABF	FASTA	683	74,513
	10 20 30 40 50 60 MRQKLLITFL ILITFTVSLT LFPVNVRADV VITSNQTGTH GGYNFEYWKD TGNGTMVLKD 70 80 90 100 110 120 GGAFSCEWSN INNILFRKGF KYDETKTHDQ LGYITVTYSC NYQPNGNSYL GVYGWTSNPL 130 140 150 160 170 180 VEYYIIESWG TWRPPGATPK GTITVDGGTY EIYETTRVNQ PSIKGTATFQ QYWSVRTSKR 190 200 210 220 230 240 TSGTISVTEH FKAWERLGMK MGKMYEVALV VEGYQSSGKA DVTSMTITVG NAPSTSSPPG 250 260 270 280 290 300 PTPEPTPRSA FSKIEAEEYN SLKSSTIQTI GTSDGGSGIG YIESGDYLVF NKINFGNGAN 310 320 330 340 350 360 SFKARVASGA DTPTNIQLRL GSPTGTLIGT LTVASTGGWN NYEEKSCSIT NTTGQHDLYL 370 380 390 400 410 420 VFSGPVNIDY FIFDSNGVNP TPTSQPQQGQ VLGDLNGDKQ VNSTDYTALK RHLLNITRLS 430 440 450 460 470 480 GTALANADLN GDGKVDSTDL MILHRYLLGI ISSFPRSNPQ PSSNPQPSSN PQPTINPNAK 490 500 510 520 530 540 LVALTFDDGP DNVLTARVLD KLDKYNVKAT FMVVGQRVND STAAIIRRMV NSGHEIGNHS 550 560 570 580 590 600 WSYSGMANMS PDQIRKSIAD TNAVIQKYAG TTPKFFRPPN LETSPTLFNN VDLVFVGGLT 610 620 630 640 650 660 ANDWIPSTTA EQRAAAVING VRDGTIILLH DVQPEPHPTP EALDIIIPTL KSRGYEFVTL 670 680 TELFTLKGVP IDPSVKRMYN SVP

References

[1]	"Nucleotide sequences of two contiguous and highly homologous xylanase genes xynA and xynB and characterization of XynA from Clostridium thermocellum." Hayashi H., Takehara M., Hattori T., Kimura T., Karita S., Sakka K., Ohmiya K. Appl. Microbiol. Biotechnol. 51:348-357(1999) [PubMed: 10222584] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: F1 EMBL BAA33543.1.
[2]	"Structure and activity of two metal ion-dependent acetylxylan esterases involved in plant cell wall degradation reveals a close similarity to peptidoglycan deacetylases." Taylor E.J., Gloster T.M., Turkenburg J.P., Vincent F., Brzozowski A.M., Dupont C., Shareck F., Centeno M.S., Prates J.A., Puchart V., Ferreira L.M., Fontes C.M., Biely P., Davies G.J. J. Biol. Chem. 281:10968-10975(2006) [PubMed: 16431911] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 480-683.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB010958 Genomic DNA. Translation: BAA33543.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C71	X-ray	1.05	A	480-683	[»]
2C79	X-ray	1.50	A	480-683	[»]

ProteinModelPortal

O87119.

SMR

O87119. Positions 31-233, 251-376, 480-683.

ModBase

Search...

Protein family/group databases

CAZy

CBM6. Carbohydrate-Binding Module Family 6.
GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR006584. Cellulose-bd_IV.
IPR005084. CMB_fam6.
IPR008985. ConA-like_lec_gl.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR008979. Galactose-bd-like.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12_cat.
IPR018208. Glyco_hydro_11_AS.
IPR002509. Polysac_deacetylase.
[Graphical view]

Gene3D

G3DSA:1.10.1330.10. Cellulos_enz_dockerin_1. 1 hit.
G3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.
G3DSA:3.20.20.370. Polysac_deacetylase. 1 hit.

Pfam

PF03422. CBM_6. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00457. Glyco_hydro_11. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view]

PRINTS

PR00911. GLHYDRLASE11.

SMART

SM00606. CBD_IV. 1 hit.
[Graphical view]

SUPFAM

SSF63446. Cellulos_enz_dockerin_1. 1 hit.
SSF49899. ConA_like_lec_gl. 1 hit.
SSF49785. Gal_bind_like. 1 hit.
SSF88713. Glyco_hydro/deAcase_b/a-brl. 1 hit.

PROSITE

PS51175. CBM6. 1 hit.
PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

O87119_CLOTM

Accession

Primary (citable) accession number: O87119

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1998
Last sequence update:	November 1, 1998
Last modified:	October 19, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)