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Protein

Xylose isomerase

Gene

xylA

Organism
Streptomyces diastaticus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in D-xylose catabolism.

Catalytic activityi

D-xylopyranose = D-xylulose.

Cofactori

Co2+Note: Binds 2 cobalt ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei54By similarity1
Active sitei57By similarity1
Metal bindingi181Cobalt 11
Metal bindingi217Cobalt 11
Metal bindingi217Cobalt 21
Metal bindingi220Cobalt 21
Metal bindingi245Cobalt 11
Metal bindingi255Cobalt 21
Metal bindingi257Cobalt 21
Metal bindingi287Cobalt 11

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Pentose shunt, Xylose metabolism

Keywords - Ligandi

Cobalt, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Xylose isomerase (EC:5.3.1.5)
Gene namesi
Name:xylA
OrganismiStreptomyces diastaticus
Taxonomic identifieri1956 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001957991 – 388Xylose isomeraseAdd BLAST388

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1388
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 9Combined sources3
Beta strandi11 – 14Combined sources4
Helixi15 – 18Combined sources4
Helixi36 – 46Combined sources11
Beta strandi50 – 54Combined sources5
Helixi55 – 58Combined sources4
Helixi65 – 82Combined sources18
Beta strandi85 – 90Combined sources6
Beta strandi94 – 96Combined sources3
Helixi97 – 99Combined sources3
Helixi109 – 129Combined sources21
Beta strandi132 – 136Combined sources5
Beta strandi141 – 148Combined sources8
Helixi151 – 172Combined sources22
Beta strandi178 – 180Combined sources3
Beta strandi184 – 193Combined sources10
Helixi196 – 203Combined sources8
Beta strandi206 – 208Combined sources3
Helixi209 – 211Combined sources3
Beta strandi212 – 214Combined sources3
Helixi218 – 222Combined sources5
Turni223 – 225Combined sources3
Helixi228 – 237Combined sources10
Beta strandi251 – 254Combined sources4
Beta strandi260 – 264Combined sources5
Helixi265 – 278Combined sources14
Beta strandi284 – 286Combined sources3
Helixi296 – 322Combined sources27
Helixi324 – 332Combined sources9
Helixi335 – 339Combined sources5
Turni342 – 345Combined sources4
Helixi347 – 350Combined sources4
Helixi354 – 356Combined sources3
Turni357 – 359Combined sources3
Helixi362 – 367Combined sources6
Helixi372 – 384Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CLKX-ray1.90A2-388[»]
1QT1X-ray1.85A/B2-388[»]
ProteinModelPortaliP50910.
SMRiP50910.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50910.

Family & Domainsi

Sequence similaritiesi

Belongs to the xylose isomerase family.Curated

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00455. Xylose_isom_A. 1 hit.
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.

P50910-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYQPTPEDK FTFGLWTVGW QGRDPFGDAT RGALDPAESV RRLAELGAHG
60 70 80 90 100
VTFHDDDLIP FGATDSERAE HIKRFRQGLD ETGMKVPMAT TNLFTHPVFK
110 120 130 140 150
DGGFTANDRD VRRYAVRKTI RNIDLAVELG AQTYVAWGGR EGAESGAAKD
160 170 180 190 200
VRVALDRMKE AFDLLGEYVT SQGYDTPFAI EPKPNEPRGD ILLPTIGHAL
210 220 230 240 250
AFIDGLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK LFHIDLNGQS
260 270 280 290 300
GIKYDQDLRF GPGDLAAAFW LVDLLESAGY EGPRHFDFKP PRTEDFDGVW
310 320 330 340 350
ASAAGCMRNY LILKERAAAF RADPEVQEAL RAARLDELAQ PTAGDGLQAL
360 370 380
LPDRSAFEDF DPDAAAARGM AFERLDQLAM DHLLGARG
Length:388
Mass (Da):42,676
Last modified:October 1, 1996 - v1
Checksum:iEFB9DA125AB1DEB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S73809 Genomic DNA. Translation: AAB32873.1.
PIRiJC1031.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S73809 Genomic DNA. Translation: AAB32873.1.
PIRiJC1031.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CLKX-ray1.90A2-388[»]
1QT1X-ray1.85A/B2-388[»]
ProteinModelPortaliP50910.
SMRiP50910.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP50910.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00455. Xylose_isom_A. 1 hit.
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...

Entry informationi

Entry nameiXYLA_STRDI
AccessioniPrimary (citable) accession number: P50910
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.