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P31434 (XYLS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-xylosidase

EC=3.2.1.177
Gene names
Name:yicI
Ordered Locus Names:b3656, JW3631
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length772 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Catalytic activity

Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose. Ref.5

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. Ref.4

Binary interactions

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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P31434 [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

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: CATALYTIC ACTIVITY, 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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10328 Genomic DNA. Translation: AAA62009.1.
U00096 Genomic DNA. Translation: AAC76680.1.
AP009048 Genomic DNA. Translation: BAE77637.1.
PIRB65167.
RefSeqNP_418113.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP31434.
SMRP31434. Positions 1-772.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-12433N.
IntActP31434. 2 interactions.

Protein family/group databases

CAZyGH31. Glycoside Hydrolase Family 31.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000003933; EBESCP00000003933; EBESCG00000003218.
EBESCT00000018187; EBESCP00000017478; EBESCG00000017242.
GeneID948169.
GenomeReviewsGene locus JW3631 in contig AP009048_GR.
Gene locus b3656 in contig U00096_GR.
KEGGecj:JW3631.
eco:b3656.
PATRIC32122799. VBIEscCol129921_3776.

Organism-specific databases

EchoBASEEB1636.
EcoGeneEG11685. yicI.

Phylogenomic databases

eggNOGCOG1501.
GeneTreeEBGT00050000011402.
HOGENOMHBG312625.
OMAQYMLGDS.
PhylomeDBP31434.
ProtClustDBPRK10658.

Enzyme and pathway databases

BioCycEcoCyc:EG11685-MONOMER.
MetaCyc:EG11685-MONOMER.

Gene expression databases

GenevestigatorP31434.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR011013. Glyco_hydro-type_carb-bd.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 2 hits.
KOK01811.
PANTHERPTHR22762. Glyco_hydro_31. 1 hit.
PfamPF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMSSF74650. Gal_mut_like. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00129. GLYCOSYL_HYDROL_F31_1. False negative.
PS00707. GLYCOSYL_HYDROL_F31_2. False negative.
[Graphical view]
ProtoNetSearch...

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: January 25, 2012
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families