O52780 (O52780_CLOTM) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Xylanase U EMBL AAC04579.1

Gene names

Name:

xynU EMBL AAC04579.1

Organism

Clostridium thermocellum EMBL AAC04579.1

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 AAC04579.1
Ligand	Calcium PDB 1UXX PDB 1GMM Metal-binding PDB 1UXX PDB 1GMM
Technical term	3D-structure PDB 1UXX PDB 1GMM
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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Metal binding	255	1	Calcium PDB 1UXX PDB 1GMM
	Metal binding	257	1	Calcium PDB 1UXX PDB 1GMM
	Metal binding	277	1	Calcium; via carbonyl oxygen PDB 1UXX PDB 1GMM
	Metal binding	369	1	Calcium PDB 1UXX PDB 1GMM

Sequences

	Sequence		Length	Mass (Da)
	O52780 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 714BB16E0C9820A2	FASTA	683	74,530
	10 20 30 40 50 60 MRQKLLVTFL ILITFTVSLT LFPVNVRADV VITSNQTGTH GGYNFEYWKD TGNGTMVLKD 70 80 90 100 110 120 GGAFSCEWSN INNILFRKGF KYDETKRHDQ 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 FSKIESEEYN 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 TTPKFFRAPN LETSPTLFNN VDLVFVGGLT 610 620 630 640 650 660 ANDWIPSTTA EQRAGAVING VRDGTIILLH DVQPEPHPTP EALDIIIPTL KSRGYEFVTL 670 680 TELFTLKGVP IDPSVKRMYN SVP

References

[1]	Fernandes A.C., Fontes C.M.G.A., Clarke J.H., Hazlewood G.P., Gilbert H.J., Fernandes T.H., Ferreira L.M.A. Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[2]	"The crystal structure of the family 6 carbohydrate binding module from Cellvibrio mixtus endoglucanase 5a in complex with oligosaccharides reveals two distinct binding sites with different ligand specificities." Pires V.M., Henshaw J.L., Prates J.A., Bolam D.N., Ferreira L.M., Fontes C.M., Henrissat B., Planas A., Gilbert H.J., Czjzek M. J. Biol. Chem. 279:21560-21568(2004) [PubMed: 15010454] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 248-380 IN COMPLEX WITH CALCIUM.
[3]	"The location of the ligand-binding site of carbohydrate-binding modules that have evolved from a common sequence is not conserved." Czjzek M., Bolam D.N., Mosbah A., Allouch J., Fontes C.M., Ferreira L.M., Bornet O., Zamboni V., Darbon H., Smith N.L., Black G.W., Henrissat B., Gilbert H.J. J. Biol. Chem. 276:48580-48587(2001) [PubMed: 11673472] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 248-380 IN COMPLEX WITH CALCIUM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF047761 Genomic DNA. Translation: AAC04579.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GMM	X-ray	2.00	A	248-380	[»]
1UXX	X-ray	1.60	X	248-380	[»]

ProteinModelPortal

O52780.

SMR

O52780. 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

O52780_CLOTM

Accession

Primary (citable) accession number: O52780

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 1998
Last sequence update:	June 1, 1998
Last modified:	October 19, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)