Alpha-L-fucosidase, putative - Thermotoga maritima

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Q9WYE2 (Q9WYE2_THEMA) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 62. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Submitted name:
Alpha-L-fucosidase, putative EMBL AAD35394.1

Gene names

Ordered Locus Names:

TM_0306

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	449 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Technical term	3D-structure PDB 2WSP PDB 1HL9 PDB 1HL8 PDB 1ODU PDB 2ZX5 PDB 2ZX7 PDB 2ZX6 PDB 2ZX9 PDB 2ZX8 PDB 2ZWZ PDB 2ZXA PDB 2ZXB PDB 2ZXD PDB 2ZWY Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fucose metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	alpha-L-fucosidase activity Inferred from electronic annotation. Source: InterPro cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Region

66 – 67

Fucose binding PDB 2WSP

Region

128 – 129

Fucose binding PDB 2WSP

Sites

Binding site

Fucose PDB 2WSP

Binding site

290

Fucose PDB 2WSP

Amino acid modifications

Modified residue

338

N6-carboxylysine PDB 1HL9 PDB 1HL8

Sequences

Sequence

Length

Mass (Da)

Tools

Q9WYE2 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: B213C72A1ED9EA5C
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FASTA

449

52,205

        10         20         30         40         50         60 
MISMKPRYKP DWESLREHTV PKWFDKAKFG IFIHWGIYSV PGWATPTGEL GKVPMDAWFF 

        70         80         90        100        110        120 
QNPYAEWYEN SLRIKESPTW EYHVKTYGEN FEYEKFADLF TAEKWDPQEW ADLFKKAGAK 

       130        140        150        160        170        180 
YVIPTTKHHD GFCLWGTKYT DFNSVKRGPK RDLVGDLAKA VREAGLRFGV YYSGGLDWRF 

       190        200        210        220        230        240 
TTEPIRYPED LSYIRPNTYE YADYAYKQVM ELVDLYLPDV LWNDMGWPEK GKEDLKYLFA 

       250        260        270        280        290        300 
YYYNKHPEGS VNDRWGVPHW DFKTAEYHVN YPGDLPGYKW EFTRGIGLSF GYNRNEGPEH 

       310        320        330        340        350        360 
MLSVEQLVYT LVDVVSKGGN LLLNVGPKGD GTIPDLQKER LLGLGEWLRK YGDAIYGTSV 

       370        380        390        400        410        420 
WERCCAKTED GTEIRFTRKC NRIFVIFLGI PTGEKIVIED LNLSAGTVRH FLTGERLSFK 

       430        440 
NVGKNLEITV PKKLLETDSI TLVLEAVEE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis." Sulzenbacher G., Bignon C., Nishimura T., Tarling C.A., Withers S.G., Henrissat B., Bourne Y. J. Biol. Chem. 279:13119-13128(2004) [PubMed: 14715651] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), CARBOXYLATION AT LYS-338.
[3]	"Structural basis of alpha-fucosidase inhibition by iminocyclitols with K(i) values in the micro- to picomolar range." Wu H.J., Ho C.W., Ko T.P., Popat S.D., Lin C.H., Wang A.H. Angew. Chem. Int. Ed. 49:337-340(2010) [PubMed: 19967696] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
[4]	"beta-Glycosyl azides as substrates for alpha-glycosynthases: preparation of efficient alpha-L-fucosynthases." Cobucci-Ponzano B., Conte F., Bedini E., Corsaro M.M., Parrilli M., Sulzenbacher G., Lipski A., Dal Piaz F., Lepore L., Rossi M., Moracci M. Chem. Biol. 16:1097-1108(2009) [PubMed: 19875083] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH FUCOSE.
[5]	"Structural Basis of alpha-Fucosidase Inhibition by Iminocyclitols with Ki Ranging from Micro- to Picomolar." Wu H.-J., Ho C.-W., Ko T.P., Popat S.D., Lin C.-H., Wang A.H.-J. Submitted (DEC-2008) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000512 Genomic DNA. Translation: AAD35394.1.

PIR

G72393.

RefSeq

NP_228118.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HL8	X-ray	2.40	A/B	1-449	[»]
1HL9	X-ray	2.25	A/B	1-449	[»]
1ODU	X-ray	2.80	A/B	1-449	[»]
2WSP	X-ray	2.65	A/B	1-449	[»]
2ZWY	X-ray	2.75	A/B	1-449	[»]
2ZWZ	X-ray	2.36	A/B	1-449	[»]
2ZX5	X-ray	2.65	A/B	1-449	[»]
2ZX6	X-ray	2.42	A/B	1-449	[»]
2ZX7	X-ray	2.48	A/B	1-449	[»]
2ZX8	X-ray	2.33	A/B	1-449	[»]
2ZX9	X-ray	2.62	A/B	1-449	[»]
2ZXA	X-ray	2.57	A/B	1-449	[»]
2ZXB	X-ray	2.61	A/B	1-449	[»]
2ZXD	X-ray	2.15	A/B	1-449	[»]

ProteinModelPortal

Q9WYE2.

SMR

Q9WYE2. Positions 7-448.

ModBase

Search...

Protein family/group databases

CAZy

GH29. Glycoside Hydrolase Family 29.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

897238.

GenomeReviews

Gene locus TM_0306 in contig AE000512_GR.

KEGG

tma:TM0306.

NMPDR

fig|243274.1.peg.302.

PATRIC

23935491. VBITheMar51294_0311.

TIGR

TM_0306.

Phylogenomic databases

HOGENOM

HBG515484.

OMA

LAWLYNK.

ProtClustDB

CLSK2460115.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_0306-MONOMER.

BRENDA

3.2.1.51. 16699.

Family and domain databases

InterPro

IPR013780. Glyco_hydro_13_b.
IPR000933. Glyco_hydro_29.
IPR016286. Glyco_hydro_29_sub.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

K01206.

PANTHER

PTHR10030. Glyco_hydro_29. 1 hit.

Pfam

PF01120. Alpha_L_fucos. 1 hit.
[Graphical view]

PIRSF

PIRSF001092. Alpha-L-fucosidase. 1 hit.

PRINTS

PR00741. GLHYDRLASE29.

SMART

SM00812. Alpha_L_fucos. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Entry information

Entry name

Q9WYE2_THEMA

Accession

Primary (citable) accession number: Q9WYE2

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1999
Last sequence update:	November 1, 1999
Last modified:	December 14, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

Ontologies

Sequence annotation (Features)

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information