Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P31434 (XYLS_ECOLI)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Alpha-xylosidase
    EC=3.2.1.-
Gene names
Name: yicI
Ordered Locus Names: b3656, JW3631
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

Protein attributes

Sequence length772 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Can catalyzes the transfer of alpha-xylosyl residue from alpha-xyloside to xylose, glucose, mannose, fructose, maltose, isomaltose, nigerose, kojibiose, sucrose and trehalose. Ref.4 Ref.6

Subunit structure

Homohexamer. Ref.4 Ref.6

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

biophysicochemical properties

pH dependence:

Optimum pH is 7.0.

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

groLP0A6F51EBI-1122922,EBI-543750
narLP0AF281EBI-1122922,EBI-1122899

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 772772Alpha-xylosidase
PRO_0000185371

Sites

Active site4161 Ref.6
Active site4191 Ref.6
Active site4821Proton donor Ref.6

Experimental info

Mutagenesis307 – 3082CF → ID: Converts the enzyme to have alpha-glucosidase activity. Ref.5

Secondary structure

1 ............................................................................................................................................ 772
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P31434-1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 6F2A02E4B5403772

FASTA77288,079
        10         20         30         40         50         60 
MKISDGNWLI QPGLNLIHPL QVFEVEQQDN EMVVYAAPRD VRERTWQLDT PLFTLRFFSP 

        70         80         90        100        110        120 
QEGIVGVRIE HFQGALNNGP HYPLNILQDV KVTIENTERY AEFKSGNLSA RVSKGEFWSL 

       130        140        150        160        170        180 
DFLRNGERIT GSQVKNNGYV QDTNNQRNYM FERLDLGVGE TVYGLGERFT ALVRNGQTVE 

       190        200        210        220        230        240 
TWNRDGGTST EQAYKNIPFY MTNRGYGVLV NHPQCVSFEV GSEKVSKVQF SVESEYLEYF 

       250        260        270        280        290        300 
VIDGPTPKAV LDRYTRFTGR PALPPAWSFG LWLTTSFTTN YDEATVNSFI DGMAERNLPL 

       310        320        330        340        350        360 
HVFHFDCFWM KAFQWCDFEW DPLTFPDPEG MIRRLKAKGL KICVWINPYI GQKSPVFKEL 

       370        380        390        400        410        420 
QEKGYLLKRP DGSLWQWDKW QPGLAIYDFT NPDACKWYAD KLKGLVAMGV DCFKTDFGER 

       430        440        450        460        470        480 
IPTDVQWFDG SDPQKMHNHY AYIYNELVWN VLKDTVGEEE AVLFARSASV GAQKFPVHWG 

       490        500        510        520        530        540 
GDCYANYESM AESLRGGLSI GLSGFGFWSH DIGGFENTAP AHVYKRWCAF GLLSSHSRLH 

       550        560        570        580        590        600 
GSKSYRVPWA YDDESCDVVR FFTQLKCRMM PYLYREAARA NARGTPMMRA MMMEFPDDPA 

       610        620        630        640        650        660 
CDYLDRQYML GDNVMVAPVF TEAGDVQFYL PEGRWTHLWH NDELDGSRWH KQQHGFLSLP 

       670        680        690        700        710        720 
VYVRDNTLLA LGNNDQRPDY VWHEGTAFHL FNLQDGHEAV CEVPAADGSV IFTLKAARTG 

       730        740        750        760        770 
NTITVTGAGE AKNWTLCLRN VVKVNGLQDG SQAESEQGLV VKPQGNALTI TL

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
Genomics 16:551-561(1993) [PubMed: 7686882] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Overexpression and characterization of two unknown proteins, YicI and YihQ, originated from Escherichia coli."
Okuyama M., Mori H., Chiba S., Kimura A.
Protein Expr. Purif. 37:170-179(2004) [PubMed: 15294295] [Abstract]
Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
[5]"Structural elements to convert Escherichia coli alpha-xylosidase (YicI) into alpha-glucosidase."
Okuyama M., Kaneko A., Mori H., Chiba S., Kimura A.
FEBS Lett. 580:2707-2711(2006) [PubMed: 16631751] [Abstract]
Cited for: MUTAGENESIS OF 307-CYS-PHE-308.
[6]"Mechanistic and structural analysis of a family 31 alpha-glycosidase and its glycosyl-enzyme intermediate."
Lovering A.L., Lee S.S., Kim Y.-W., Withers S.G., Strynadka N.C.J.
J. Biol. Chem. 280:2105-2115(2005) [PubMed: 15501829] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, SUBUNIT, ACTIVE SITES.
[7]"Crystal structure of alpha-xylosidase from Escherichia coli."
Ose T., Kitamura M., Okuyama M., Mori H., Kimura A., Watanabe N., Yao M., Tanaka I.
Submitted (MAY-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Hide | Top

Cross-references

Sequence databases

L10328 Genomic DNA. Translation: AAA62009.1.
U00096 Genomic DNA. Translation: AAC76680.1.
AP009048 Genomic DNA. Translation: BAE77637.1.
PIRB65167.
RefSeqAP_004136.1.
NP_418113.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1WE5X-ray2.40A/B/C/D/E/F1-772[»]
1XSIX-ray2.20A/B/C/D/E/F1-772[»]
1XSJX-ray2.10A/B/C/D/E/F1-772[»]
1XSKX-ray2.20A/B/C/D/E/F1-772[»]
2F2HX-ray1.95A/B/C/D/E/F1-772[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP31434. 2 interactions.

Protein family/group databases

CAZyGH31. Glycoside Hydrolase Family 31.

Genome annotation databases

GeneID948169.
GenomeReviewsGene locus JW3631 in contig AP009048_GR.
Gene locus b3656 in contig U00096_GR.
KEGGecj:JW3631.
eco:b3656.

Organism-specific databases

EchoBASEEB1636.
EcoGeneEG11685. yicI.
CMRSearch...

Phylogenomic databases

HOGENOMP31434.
OMAP31434. GNEMVVY.

Enzyme and pathway databases

BioCycEcoCyc:EG11685-MON.
MetaCyc:EG11685-MON.

Family and domain databases

InterProIPR000322. Glyco_hydro_31.
[Graphical view]
PANTHERPTHR22762. Glyco_hydro_31. 1 hit.
PfamPF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
PROSITEPS00129. GLYCOSYL_HYDROL_F31_1. False negative.
PS00707. GLYCOSYL_HYDROL_F31_2. False negative.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameXYLS_ECOLI
AccessionPrimary (citable) accession number: P31434
Secondary accession number(s): P76723, Q2M7W9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 15, 1998
Last modified: June 16, 2009
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents