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Protein

Alpha-xylosidase

Gene

yicI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Can catalyze the transfer of alpha-xylosyl residue from alpha-xyloside to xylose, glucose, mannose, fructose, maltose, isomaltose, nigerose, kojibiose, sucrose and trehalose.2 Publications

Catalytic activityi

Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.1 Publication

pH dependencei

Optimum pH is 7.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei416 – 4161Nucleophile1 Publication
Active sitei419 – 41911 Publication
Active sitei482 – 4821Proton donor1 Publication

GO - Molecular functioni

  • alpha-D-xyloside xylohydrolase Source: UniProtKB-EC
  • carbohydrate binding Source: InterPro
  • identical protein binding Source: EcoCyc
  • xyloglucan 1,6-alpha-xylosidase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciEcoCyc:EG11685-MONOMER.
ECOL316407:JW3631-MONOMER.
MetaCyc:EG11685-MONOMER.
BRENDAi3.2.1.177. 2026.
SABIO-RKP31434.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-xylosidase (EC:3.2.1.177)
Gene namesi
Name:yicI
Ordered Locus Names:b3656, JW3631
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11685. yicI.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi307 – 3082CF → ID: Converts the enzyme to have alpha-glucosidase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 772772Alpha-xylosidasePRO_0000185371Add
BLAST

Proteomic databases

PaxDbiP31434.
PRIDEiP31434.

Interactioni

Subunit structurei

Homohexamer.2 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262572. 5 interactions.
DIPiDIP-12433N.
IntActiP31434. 2 interactions.
STRINGi511145.b3656.

Structurei

Secondary structure

1
772
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni6 – 83Combined sources
Beta strandi14 – 174Combined sources
Beta strandi21 – 288Combined sources
Beta strandi31 – 399Combined sources
Helixi44 – 463Combined sources
Beta strandi47 – 504Combined sources
Beta strandi53 – 586Combined sources
Beta strandi64 – 718Combined sources
Beta strandi92 – 965Combined sources
Beta strandi98 – 1058Combined sources
Beta strandi108 – 1136Combined sources
Beta strandi115 – 1173Combined sources
Beta strandi119 – 1246Combined sources
Beta strandi127 – 1337Combined sources
Beta strandi136 – 1427Combined sources
Turni143 – 1464Combined sources
Beta strandi147 – 1559Combined sources
Beta strandi162 – 1676Combined sources
Beta strandi177 – 1804Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi194 – 2029Combined sources
Beta strandi205 – 2106Combined sources
Beta strandi217 – 2248Combined sources
Beta strandi227 – 24317Combined sources
Helixi247 – 25812Combined sources
Helixi266 – 2694Combined sources
Beta strandi270 – 2745Combined sources
Beta strandi277 – 2793Combined sources
Helixi283 – 29513Combined sources
Beta strandi302 – 3054Combined sources
Helixi307 – 3093Combined sources
Turni322 – 3243Combined sources
Helixi328 – 33710Combined sources
Beta strandi341 – 3466Combined sources
Beta strandi348 – 3503Combined sources
Helixi357 – 3637Combined sources
Beta strandi372 – 3743Combined sources
Beta strandi377 – 3815Combined sources
Beta strandi384 – 3874Combined sources
Helixi392 – 40716Combined sources
Beta strandi412 – 4154Combined sources
Beta strandi423 – 4264Combined sources
Helixi433 – 45321Combined sources
Turni454 – 4563Combined sources
Helixi458 – 4603Combined sources
Beta strandi463 – 4664Combined sources
Helixi472 – 4743Combined sources
Beta strandi484 – 4863Combined sources
Helixi487 – 50115Combined sources
Turni502 – 5043Combined sources
Beta strandi508 – 5114Combined sources
Beta strandi515 – 5173Combined sources
Helixi521 – 53212Combined sources
Beta strandi534 – 5396Combined sources
Beta strandi542 – 5443Combined sources
Helixi548 – 5503Combined sources
Helixi553 – 58331Combined sources
Beta strandi587 – 5893Combined sources
Helixi591 – 5944Combined sources
Helixi599 – 6013Combined sources
Beta strandi608 – 6103Combined sources
Turni611 – 6133Combined sources
Beta strandi614 – 6163Combined sources
Beta strandi621 – 6233Combined sources
Beta strandi625 – 6306Combined sources
Beta strandi632 – 6376Combined sources
Turni638 – 6403Combined sources
Beta strandi643 – 6453Combined sources
Beta strandi647 – 6537Combined sources
Beta strandi661 – 6633Combined sources
Beta strandi665 – 6717Combined sources
Beta strandi678 – 6803Combined sources
Beta strandi687 – 6915Combined sources
Beta strandi698 – 7047Combined sources
Beta strandi710 – 71910Combined sources
Beta strandi722 – 7298Combined sources
Beta strandi735 – 7384Combined sources
Beta strandi745 – 7539Combined sources
Beta strandi756 – 7583Combined sources
Beta strandi760 – 7667Combined sources
Beta strandi770 – 7723Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP31434.
SMRiP31434. Positions 1-772.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31434.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated

Phylogenomic databases

eggNOGiENOG4105CJQ. Bacteria.
COG1501. LUCA.
HOGENOMiHOG000221907.
InParanoidiP31434.
KOiK01811.
OMAiTPDLYKR.
OrthoDBiEOG6Z99WN.
PhylomeDBiP31434.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
InterProiIPR013785. Aldolase_TIM.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.

Sequencei

Sequence statusi: Complete.

P31434-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKISDGNWLI QPGLNLIHPL QVFEVEQQDN EMVVYAAPRD VRERTWQLDT
60 70 80 90 100
PLFTLRFFSP QEGIVGVRIE HFQGALNNGP HYPLNILQDV KVTIENTERY
110 120 130 140 150
AEFKSGNLSA RVSKGEFWSL DFLRNGERIT GSQVKNNGYV QDTNNQRNYM
160 170 180 190 200
FERLDLGVGE TVYGLGERFT ALVRNGQTVE TWNRDGGTST EQAYKNIPFY
210 220 230 240 250
MTNRGYGVLV NHPQCVSFEV GSEKVSKVQF SVESEYLEYF VIDGPTPKAV
260 270 280 290 300
LDRYTRFTGR PALPPAWSFG LWLTTSFTTN YDEATVNSFI DGMAERNLPL
310 320 330 340 350
HVFHFDCFWM KAFQWCDFEW DPLTFPDPEG MIRRLKAKGL KICVWINPYI
360 370 380 390 400
GQKSPVFKEL QEKGYLLKRP DGSLWQWDKW QPGLAIYDFT NPDACKWYAD
410 420 430 440 450
KLKGLVAMGV DCFKTDFGER IPTDVQWFDG SDPQKMHNHY AYIYNELVWN
460 470 480 490 500
VLKDTVGEEE AVLFARSASV GAQKFPVHWG GDCYANYESM AESLRGGLSI
510 520 530 540 550
GLSGFGFWSH DIGGFENTAP AHVYKRWCAF GLLSSHSRLH GSKSYRVPWA
560 570 580 590 600
YDDESCDVVR FFTQLKCRMM PYLYREAARA NARGTPMMRA MMMEFPDDPA
610 620 630 640 650
CDYLDRQYML GDNVMVAPVF TEAGDVQFYL PEGRWTHLWH NDELDGSRWH
660 670 680 690 700
KQQHGFLSLP VYVRDNTLLA LGNNDQRPDY VWHEGTAFHL FNLQDGHEAV
710 720 730 740 750
CEVPAADGSV IFTLKAARTG NTITVTGAGE AKNWTLCLRN VVKVNGLQDG
760 770
SQAESEQGLV VKPQGNALTI TL
Length:772
Mass (Da):88,079
Last modified:July 15, 1998 - v2
Checksum:i6F2A02E4B5403772
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10328 Genomic DNA. Translation: AAA62009.1.
U00096 Genomic DNA. Translation: AAC76680.1.
AP009048 Genomic DNA. Translation: BAE77637.1.
PIRiB65167.
RefSeqiNP_418113.1. NC_000913.3.
WP_000702898.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76680; AAC76680; b3656.
BAE77637; BAE77637; BAE77637.
GeneIDi948169.
KEGGiecj:JW3631.
eco:b3656.
PATRICi32122799. VBIEscCol129921_3776.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10328 Genomic DNA. Translation: AAA62009.1.
U00096 Genomic DNA. Translation: AAC76680.1.
AP009048 Genomic DNA. Translation: BAE77637.1.
PIRiB65167.
RefSeqiNP_418113.1. NC_000913.3.
WP_000702898.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP31434.
SMRiP31434. Positions 1-772.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262572. 5 interactions.
DIPiDIP-12433N.
IntActiP31434. 2 interactions.
STRINGi511145.b3656.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Proteomic databases

PaxDbiP31434.
PRIDEiP31434.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76680; AAC76680; b3656.
BAE77637; BAE77637; BAE77637.
GeneIDi948169.
KEGGiecj:JW3631.
eco:b3656.
PATRICi32122799. VBIEscCol129921_3776.

Organism-specific databases

EchoBASEiEB1636.
EcoGeneiEG11685. yicI.

Phylogenomic databases

eggNOGiENOG4105CJQ. Bacteria.
COG1501. LUCA.
HOGENOMiHOG000221907.
InParanoidiP31434.
KOiK01811.
OMAiTPDLYKR.
OrthoDBiEOG6Z99WN.
PhylomeDBiP31434.

Enzyme and pathway databases

BioCyciEcoCyc:EG11685-MONOMER.
ECOL316407:JW3631-MONOMER.
MetaCyc:EG11685-MONOMER.
BRENDAi3.2.1.177. 2026.
SABIO-RKP31434.

Miscellaneous databases

EvolutionaryTraceiP31434.
PROiP31434.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
InterProiIPR013785. Aldolase_TIM.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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).

Entry informationi

Entry nameiXYLS_ECOLI
AccessioniPrimary (citable) accession number: P31434
Secondary accession number(s): P76723, Q2M7W9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 15, 1998
Last modified: April 13, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.