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Protein

Xylose isomerase

Gene

xylA

Organism
Streptomyces olivochromogenes
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

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei54By similarity1
Active sitei57By similarity1
Metal bindingi181Magnesium 11
Metal bindingi217Magnesium 11
Metal bindingi217Magnesium 21
Metal bindingi220Magnesium 21
Metal bindingi245Magnesium 11
Metal bindingi255Magnesium 21
Metal bindingi257Magnesium 21
Metal bindingi287Magnesium 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

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi5.3.1.5. 5943.

Names & Taxonomyi

Protein namesi
Recommended name:
Xylose isomerase (EC:5.3.1.5)
Gene namesi
Name:xylA
OrganismiStreptomyces olivochromogenes
Taxonomic identifieri1963 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001958032 – 387Xylose isomeraseAdd BLAST386

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1387
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 strandi88 – 90Combined sources3
Beta strandi94 – 96Combined sources3
Helixi97 – 99Combined sources3
Helixi109 – 129Combined sources21
Beta strandi132 – 136Combined sources5
Beta strandi142 – 145Combined sources4
Helixi146 – 148Combined sources3
Helixi151 – 172Combined sources22
Beta strandi177 – 180Combined sources4
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 strandi262 – 264Combined sources3
Helixi265 – 278Combined sources14
Beta strandi284 – 286Combined sources3
Helixi296 – 322Combined sources27
Helixi324 – 332Combined sources9
Helixi335 – 338Combined sources4
Helixi347 – 352Combined sources6
Helixi354 – 356Combined sources3
Turni357 – 359Combined sources3
Helixi362 – 367Combined sources6
Helixi372 – 383Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MUWX-ray0.86A2-387[»]
1S5MX-ray0.98A2-387[»]
1S5NX-ray0.95A2-387[»]
1XYAX-ray1.81A/B2-387[»]
1XYBX-ray1.96A/B2-387[»]
1XYCX-ray2.19A/B2-387[»]
1XYLX-ray1.80A/B2-387[»]
1XYMX-ray1.80A/B2-387[»]
2GYIX-ray1.60A/B2-387[»]
ProteinModelPortaliP15587.
SMRiP15587.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15587.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15587-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYQPTPEDR FTFGLWTVGW QGRDPFGDAT RPALDPVETV QRLAELGAHG
60 70 80 90 100
VTFHDDDLIP FGSSDTERES HIKRFRQALD ATGMTVPMAT TNLFTHPVFK
110 120 130 140 150
DGGFTANDRD VRRYALRKTI RNIDLAVELG AKTYVAWGGR EGAESGAAKD
160 170 180 190 200
VRVALDRMKE AFDLLGEYVT SQGYDTRFAI EPKPNEPRGD ILLPTVGHAL
210 220 230 240 250
AFIERLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK LFHIDLNGQS
260 270 280 290 300
GIKYDQDLRF GAGDLRAAFW LVDLLESAGY EGPRHFDFKP PRTEDIDGVW
310 320 330 340 350
ASAAGCMRNY LILKERAAAF RADPEVQEAL RASRLDELAQ PTAADGVQEL
360 370 380
LADRTAFEDF DVDAAAARGM AFERLDQLAM DHLLGAR
Length:387
Mass (Da):42,923
Last modified:January 23, 2007 - v3
Checksum:i83CCE206015B178D
GO

Sequence databases

PIRiS28986.

Cross-referencesi

Sequence databases

PIRiS28986.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MUWX-ray0.86A2-387[»]
1S5MX-ray0.98A2-387[»]
1S5NX-ray0.95A2-387[»]
1XYAX-ray1.81A/B2-387[»]
1XYBX-ray1.96A/B2-387[»]
1XYCX-ray2.19A/B2-387[»]
1XYLX-ray1.80A/B2-387[»]
1XYMX-ray1.80A/B2-387[»]
2GYIX-ray1.60A/B2-387[»]
ProteinModelPortaliP15587.
SMRiP15587.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi5.3.1.5. 5943.

Miscellaneous databases

EvolutionaryTraceiP15587.

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_STROL
AccessioniPrimary (citable) accession number: P15587
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 109 of the entry and version 3 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.