Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Xylose isomerase

Gene

xylA

Organism
Streptomyces sp. SK
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-xylopyranose = D-xylulose.UniRule annotationSAAS annotation

Cofactori

Mg2+UniRule annotationNote: Binds 2 magnesium ions per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541UniRule annotation
Active sitei57 – 571UniRule annotation
Metal bindingi181 – 1811MagnesiumCombined sources
Metal bindingi181 – 1811Magnesium 1UniRule annotation
Metal bindingi217 – 2171MagnesiumCombined sources
Metal bindingi217 – 2171Magnesium 1UniRule annotation
Metal bindingi217 – 2171Magnesium 2UniRule annotation
Metal bindingi220 – 2201Magnesium 2UniRule annotation
Metal bindingi245 – 2451MagnesiumCombined sources
Metal bindingi245 – 2451Magnesium 1UniRule annotation
Metal bindingi255 – 2551Magnesium 2UniRule annotation
Metal bindingi257 – 2571Magnesium 2UniRule annotation
Metal bindingi287 – 2871MagnesiumCombined sources
Metal bindingi287 – 2871Magnesium 1UniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. xylose isomerase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. D-xylose metabolic process Source: UniProtKB-HAMAP
  2. pentose-phosphate shunt Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

IsomeraseUniRule annotation

Keywords - Biological processi

Carbohydrate metabolism, Pentose shuntUniRule annotation, Xylose metabolismUniRule annotation

Keywords - Ligandi

MagnesiumCombined sources, Metal-bindingCombined sources

Names & Taxonomyi

Protein namesi
Recommended name:
Xylose isomeraseUniRule annotation (EC:5.3.1.5UniRule annotation)
Gene namesi
Name:xylAUniRule annotationImported
OrganismiStreptomyces sp. SKImported
Taxonomic identifieri253732 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HHLX-ray1.73A/B1-388[»]
4HHMX-ray2.15A/B/C/D/E/F/G/H1-388[»]
ProteinModelPortaliQ9ZAI3.
SMRiQ9ZAI3. Positions 2-387.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the xylose isomerase family.UniRule annotation

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00455. Xylose_isom_A.
InterProiIPR013022. Xyl_isomerase-like_TIM-brl.
IPR013453. XylA_actinobac.
IPR001998. Xylose_isomerase.
[Graphical view]
PfamiPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
PRINTSiPR00688. XYLOSISMRASE.
SUPFAMiSSF51658. SSF51658. 1 hit.
TIGRFAMsiTIGR02631. xylA_Arthro. 1 hit.
PROSITEiPS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ZAI3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYQPTPEDR FTFGLWTVGW QGRDPFGDAT RPALDPVEAV QRLAELGAYG
60 70 80 90 100
VTFHDDDLIP FGASDTEREA HVKRFRQALD ATGMTVPMAT TNLFTHPVFK
110 120 130 140 150
DGAFTANDRD VRRYALRKTI RNIDLAVELG AKVYVAWGGR EGAESGAAKD
160 170 180 190 200
VRAALDRMKE AFDLLGEYVT SQGYDIRFAI EPKPNEPRGD ILLPTIGHAL
210 220 230 240 250
AFIERLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK LFHIDLNGQS
260 270 280 290 300
GIKYDQDLRF GAGDLRAAFW LVDLLESAGW EGPRHFDFKP PRTEDIDGVW
310 320 330 340 350
ASAAGCMRNY LILKERAAAF RADPEVQEAL RAARLDQLAE PTAADGLQAL
360 370 380
LADRTAYEDF DVDAAAARGM AFERLDQLAM DHLLGARG
Length:388
Mass (Da):42,946
Last modified:March 1, 2004 - v2
Checksum:i034009333C53DE5B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y15518 Genomic DNA. Translation: CAA75672.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y15518 Genomic DNA. Translation: CAA75672.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HHLX-ray1.73A/B1-388[»]
4HHMX-ray2.15A/B/C/D/E/F/G/H1-388[»]
ProteinModelPortaliQ9ZAI3.
SMRiQ9ZAI3. Positions 2-387.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00455. Xylose_isom_A.
InterProiIPR013022. Xyl_isomerase-like_TIM-brl.
IPR013453. XylA_actinobac.
IPR001998. Xylose_isomerase.
[Graphical view]
PfamiPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
PRINTSiPR00688. XYLOSISMRASE.
SUPFAMiSSF51658. SSF51658. 1 hit.
TIGRFAMsiTIGR02631. xylA_Arthro. 1 hit.
PROSITEiPS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Belghith-Srih K.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: SKImported.
  2. "Identification of critical residues for the activity and thermostability of Streptomyces sp. SK glucose isomerase."
    Ben Hlima H., Bejar S., Riguet J., Haser R., Aghajari N.
    Appl. Microbiol. Biotechnol. 97:9715-9726(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.

Entry informationi

Entry nameiQ9ZAI3_9ACTO
AccessioniPrimary (citable) accession number: Q9ZAI3
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: March 1, 2004
Last modified: January 7, 2015
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.