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XYLS_ECOLI
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-AUG-2022, entry version 149.
DE   RecName: Full=Alpha-xylosidase;
DE            EC=3.2.1.177;
GN   Name=yicI; OrderedLocusNames=b3656, JW3631;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   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 genome:
RT   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   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., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(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 MG1655
RT   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   CATALYTIC ACTIVITY, AND 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 (YicI)
RT   into alpha-glucosidase.";
RL   FEBS Lett. 580:2707-2711(2006).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, SUBUNIT, AND ACTIVE 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 and
RT   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., Yao M.,
RA   Tanaka I.;
RT   "Crystal structure of alpha-xylosidase from Escherichia coli.";
RL   Submitted (MAY-2004) to the PDB data bank.
CC   -!- FUNCTION: Can catalyze the transfer of alpha-xylosyl residue from
CC       alpha-xyloside to xylose, glucose, mannose, fructose, maltose,
CC       isomaltose, nigerose, kojibiose, sucrose and trehalose.
CC       {ECO:0000269|PubMed:15294295, ECO:0000269|PubMed:15501829}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-xylose residues
CC         with release of alpha-D-xylose.; EC=3.2.1.177;
CC         Evidence={ECO:0000269|PubMed:16631751};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:15294295};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:15294295,
CC       ECO:0000269|PubMed:15501829}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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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; NP_418113.1; NC_000913.3.
DR   RefSeq; WP_000702898.1; NZ_LN832404.1.
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   AlphaFoldDB; P31434; -.
DR   SMR; P31434; -.
DR   BioGRID; 4262572; 6.
DR   DIP; DIP-12433N; -.
DR   IntAct; P31434; 2.
DR   STRING; 511145.b3656; -.
DR   DrugBank; DB03586; (3R,4R,5S,6R)-6-Fluoro-3,4,5-trihydroxytetrahydro-2H-pyran-2-olate.
DR   DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR   DrugBank; DB03434; 3-(N-morpholino)propanesulfonic acid.
DR   DrugBank; DB04807; 4-NITROPHENYL-(6-S-ALPHA-D-XYLOPYRANOSYL)-BETA-D-GLUCOPYRANOSIDE.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   PaxDb; P31434; -.
DR   PRIDE; P31434; -.
DR   EnsemblBacteria; AAC76680; AAC76680; b3656.
DR   EnsemblBacteria; BAE77637; BAE77637; BAE77637.
DR   GeneID; 948169; -.
DR   KEGG; ecj:JW3631; -.
DR   KEGG; eco:b3656; -.
DR   PATRIC; fig|1411691.4.peg.3050; -.
DR   EchoBASE; EB1636; -.
DR   eggNOG; COG1501; Bacteria.
DR   HOGENOM; CLU_000631_10_0_6; -.
DR   InParanoid; P31434; -.
DR   OMA; QGVDCFK; -.
DR   PhylomeDB; P31434; -.
DR   BioCyc; EcoCyc:EG11685-MON; -.
DR   BioCyc; MetaCyc:EG11685-MON; -.
DR   BRENDA; 3.2.1.177; 2026.
DR   SABIO-RK; P31434; -.
DR   EvolutionaryTrace; P31434; -.
DR   PRO; PR:P31434; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0061634; F:alpha-D-xyloside xylohydrolase; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0080176; F:xyloglucan 1,6-alpha-xylosidase activity; IDA:EcoCyc.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 2.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR000322; Glyco_hydro_31.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..772
FT                   /note="Alpha-xylosidase"
FT                   /id="PRO_0000185371"
FT   ACT_SITE        416
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:15501829"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000269|PubMed:15501829"
FT   ACT_SITE        482
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000269|PubMed:15501829"
FT   MUTAGEN         307..308
FT                   /note="CF->ID: Converts the enzyme to have alpha-
FT                   glucosidase activity."
FT                   /evidence="ECO:0000269|PubMed:16631751"
FT   TURN            6..8
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          14..17
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          21..28
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          31..39
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          47..50
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          53..58
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          64..71
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          92..96
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          98..105
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          108..113
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          119..124
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          127..133
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          136..142
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   TURN            143..146
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          147..155
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          162..167
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          189..191
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          194..202
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          205..210
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          217..224
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          227..243
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           247..258
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           266..269
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          270..274
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          277..279
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           283..295
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          302..305
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           307..309
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   TURN            322..324
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           328..337
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          341..346
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          348..350
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           357..363
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          372..374
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          377..381
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          384..387
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           392..407
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          412..415
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          423..426
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           433..453
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   TURN            454..456
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           458..460
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          463..466
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           472..474
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          484..486
FT                   /evidence="ECO:0007829|PDB:1XSJ"
FT   HELIX           487..501
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   TURN            502..504
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          508..511
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          515..517
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           521..532
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          534..539
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          542..544
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           548..550
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           553..583
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          587..589
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           591..594
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   HELIX           599..601
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          608..610
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   TURN            611..613
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          614..616
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          621..623
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          625..630
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          632..637
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   TURN            638..640
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          643..645
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          647..653
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          661..663
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          665..671
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          678..680
FT                   /evidence="ECO:0007829|PDB:1XSJ"
FT   STRAND          687..691
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          698..704
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          710..719
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          722..729
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          735..738
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          745..753
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          756..758
FT                   /evidence="ECO:0007829|PDB:1XSK"
FT   STRAND          760..766
FT                   /evidence="ECO:0007829|PDB:2F2H"
FT   STRAND          770..772
FT                   /evidence="ECO:0007829|PDB:1XSI"
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
 
 
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