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