user: GUEST
width: 600


MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).

Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=Alpha-xylosidase; EC=3.2.1.-;
MyHits logo
MyHits synonymsXYLS_ECOLI , P31434 , P76723 , Q2M7W9 , 6F2A02E4B5403772
match map segment
ipfam:Gal_mutarotas_2 ipfam:Glyco_hydro_31  
Legends: 1, ACT_SITE Proton donor; 2, MUTAGEN CF->ID: Converts the enzyme to have alpha-glucosidase activity; 3, ipfam:Gal_mutarotas_2 [T]; 4, TURN; 5, STRAND; 6, HELIX.
ID   XYLS_ECOLI              Reviewed;         772 AA.
AC   P31434; P76723; Q2M7W9;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-NOV-2009, entry version 68.
DE   RecName: Full=Alpha-xylosidase;
DE            EC=3.2.1.-;
GN   Name=yicI; OrderedLocusNames=b3656, JW3631;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=93315143; PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA   Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT   "DNA sequence and analysis of 136 kilobases of the Escherichia coli
RT   genome: organizational symmetry around the origin of replication.";
RL   Genomics 16:551-561(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=15294295; DOI=10.1016/j.pep.2004.05.008;
RA   Okuyama M., Mori H., Chiba S., Kimura A.;
RT   "Overexpression and characterization of two unknown proteins, YicI and
RT   YihQ, originated from Escherichia coli.";
RL   Protein Expr. Purif. 37:170-179(2004).
RN   [5]
RP   MUTAGENESIS OF 307-CYS-PHE-308.
RX   PubMed=16631751; DOI=10.1016/j.febslet.2006.04.025;
RA   Okuyama M., Kaneko A., Mori H., Chiba S., Kimura A.;
RT   "Structural elements to convert Escherichia coli alpha-xylosidase
RT   (YicI) into alpha-glucosidase.";
RL   FEBS Lett. 580:2707-2711(2006).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, SUBUNIT, AND ACTIVE
RP   SITES.
RX   PubMed=15501829; DOI=10.1074/jbc.M410468200;
RA   Lovering A.L., Lee S.S., Kim Y.-W., Withers S.G., Strynadka N.C.J.;
RT   "Mechanistic and structural analysis of a family 31 alpha-glycosidase
RT   and its glycosyl-enzyme intermediate.";
RL   J. Biol. Chem. 280:2105-2115(2005).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RA   Ose T., Kitamura M., Okuyama M., Mori H., Kimura A., Watanabe N.,
RA   Yao M., Tanaka I.;
RT   "Crystal structure of alpha-xylosidase from Escherichia coli.";
RL   Submitted (MAY-2004) to the PDB data bank.
CC   -!- FUNCTION: Can catalyzes the transfer of alpha-xylosyl residue from
CC       alpha-xyloside to xylose, glucose, mannose, fructose, maltose,
CC       isomaltose, nigerose, kojibiose, sucrose and trehalose.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0;
CC   -!- SUBUNIT: Homohexamer.
CC   -!- INTERACTION:
CC       P0A6F5:groL; NbExp=1; IntAct=EBI-1122922, EBI-543750;
CC       P0AF28:narL; NbExp=1; IntAct=EBI-1122922, EBI-1122899;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L10328; AAA62009.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76680.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77637.1; -; Genomic_DNA.
DR   PIR; B65167; B65167.
DR   RefSeq; AP_004136.1; -.
DR   RefSeq; NP_418113.1; -.
DR   PDB; 1WE5; X-ray; 2.40 A; A/B/C/D/E/F=1-772.
DR   PDB; 1XSI; X-ray; 2.20 A; A/B/C/D/E/F=1-772.
DR   PDB; 1XSJ; X-ray; 2.10 A; A/B/C/D/E/F=1-772.
DR   PDB; 1XSK; X-ray; 2.20 A; A/B/C/D/E/F=1-772.
DR   PDB; 2F2H; X-ray; 1.95 A; A/B/C/D/E/F=1-772.
DR   PDBsum; 1WE5; -.
DR   PDBsum; 1XSI; -.
DR   PDBsum; 1XSJ; -.
DR   PDBsum; 1XSK; -.
DR   PDBsum; 2F2H; -.
DR   IntAct; P31434; 2.
DR   STRING; P31434; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   GeneID; 948169; -.
DR   GenomeReviews; AP009048_GR; JW3631.
DR   GenomeReviews; U00096_GR; b3656.
DR   KEGG; ecj:JW3631; -.
DR   KEGG; eco:b3656; -.
DR   EchoBASE; EB1636; -.
DR   EcoGene; EG11685; yicI.
DR   HOGENOM; P31434; -.
DR   OMA; GNEMVVY; -.
DR   BioCyc; EcoCyc:EG11685-MON; -.
DR   BioCyc; MetaCyc:EG11685-MON; -.
DR   Genevestigator; P31434; -.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl ...; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR000322; Glyco_hydro_31.
DR   PANTHER; PTHR22762; Glyco_hydro_31; 1.
DR   Pfam; PF01055; Glyco_hydro_31; 1.
DR   PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; FALSE_NEG.
DR   PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Glycosidase; Hydrolase.
FT   CHAIN         1    772       Alpha-xylosidase.
FT                                /FTId=PRO_0000185371.
FT   ACT_SITE    416    416
FT   ACT_SITE    419    419
FT   ACT_SITE    482    482       Proton donor.
FT   MUTAGEN     307    308       CF->ID: Converts the enzyme to have
FT                                alpha-glucosidase activity.
FT   TURN          6      8
FT   STRAND       14     17
FT   STRAND       21     28
FT   STRAND       31     39
FT   HELIX        44     46
FT   STRAND       47     50
FT   STRAND       53     58
FT   STRAND       64     71
FT   STRAND       92     96
FT   STRAND       98    105
FT   STRAND      108    113
FT   STRAND      115    117
FT   STRAND      119    124
FT   STRAND      127    133
FT   STRAND      136    142
FT   TURN        143    146
FT   STRAND      147    155
FT   STRAND      162    167
FT   STRAND      177    180
FT   STRAND      189    191
FT   STRAND      194    202
FT   STRAND      205    210
FT   STRAND      217    224
FT   STRAND      227    243
FT   HELIX       247    258
FT   HELIX       266    269
FT   STRAND      270    274
FT   STRAND      277    279
FT   HELIX       283    295
FT   STRAND      302    305
FT   HELIX       307    309
FT   TURN        322    324
FT   HELIX       328    337
FT   STRAND      341    346
FT   STRAND      348    350
FT   HELIX       355    363
FT   STRAND      372    374
FT   STRAND      377    381
FT   STRAND      384    387
FT   HELIX       392    407
FT   STRAND      412    415
FT   STRAND      423    426
FT   HELIX       433    454
FT   TURN        455    457
FT   HELIX       458    460
FT   STRAND      463    466
FT   HELIX       472    474
FT   STRAND      484    486
FT   HELIX       487    501
FT   TURN        502    504
FT   STRAND      515    517
FT   HELIX       521    532
FT   STRAND      534    539
FT   STRAND      542    544
FT   HELIX       548    550
FT   HELIX       553    583
FT   STRAND      587    589
FT   HELIX       591    594
FT   HELIX       599    601
FT   STRAND      608    610
FT   TURN        611    613
FT   STRAND      614    616
FT   STRAND      621    623
FT   STRAND      625    630
FT   STRAND      632    637
FT   TURN        638    640
FT   STRAND      643    653
FT   STRAND      661    663
FT   STRAND      665    671
FT   STRAND      687    691
FT   STRAND      698    704
FT   STRAND      708    729
FT   STRAND      735    739
FT   STRAND      744    753
FT   STRAND      758    766
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       159    218       ipfam:Gal_mutarotas_2 [T]
FT   MYHIT       240    667       ipfam:Glyco_hydro_31 [T]
SQ   SEQUENCE   772 AA;  88079 MW;  6F2A02E4B5403772 CRC64;
     MKISDGNWLI QPGLNLIHPL QVFEVEQQDN EMVVYAAPRD VRERTWQLDT PLFTLRFFSP
     QEGIVGVRIE HFQGALNNGP HYPLNILQDV KVTIENTERY AEFKSGNLSA RVSKGEFWSL
     DFLRNGERIT GSQVKNNGYV QDTNNQRNYM FERLDLGVGE TVYGLGERFT ALVRNGQTVE
     TWNRDGGTST EQAYKNIPFY MTNRGYGVLV NHPQCVSFEV GSEKVSKVQF SVESEYLEYF
     VIDGPTPKAV LDRYTRFTGR PALPPAWSFG LWLTTSFTTN YDEATVNSFI DGMAERNLPL
     HVFHFDCFWM KAFQWCDFEW DPLTFPDPEG MIRRLKAKGL KICVWINPYI GQKSPVFKEL
     QEKGYLLKRP DGSLWQWDKW QPGLAIYDFT NPDACKWYAD KLKGLVAMGV DCFKTDFGER
     IPTDVQWFDG SDPQKMHNHY AYIYNELVWN VLKDTVGEEE AVLFARSASV GAQKFPVHWG
     GDCYANYESM AESLRGGLSI GLSGFGFWSH DIGGFENTAP AHVYKRWCAF GLLSSHSRLH
     GSKSYRVPWA YDDESCDVVR FFTQLKCRMM PYLYREAARA NARGTPMMRA MMMEFPDDPA
     CDYLDRQYML GDNVMVAPVF TEAGDVQFYL PEGRWTHLWH NDELDGSRWH KQQHGFLSLP
     VYVRDNTLLA LGNNDQRPDY VWHEGTAFHL FNLQDGHEAV CEVPAADGSV IFTLKAARTG
     NTITVTGAGE AKNWTLCLRN VVKVNGLQDG SQAESEQGLV VKPQGNALTI TL
//