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P15587

- XYLA_STROL

UniProt

P15587 - XYLA_STROL

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Protein

Xylose isomerase

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

Functioni

Involved in D-xylose catabolism.UniRule annotation

Catalytic activityi

D-xylopyranose = D-xylulose.UniRule annotation

Cofactori

Binds 2 magnesium ions per subunit By similarity.UniRule annotation

Sites

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

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

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Pentose shunt, Xylose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

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

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 387386Xylose isomeraseUniRule annotationPRO_0000195803Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
387
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 93
Beta strandi11 – 144
Helixi15 – 184
Helixi36 – 4611
Beta strandi50 – 545
Helixi55 – 584
Helixi65 – 8218
Beta strandi88 – 903
Beta strandi94 – 963
Helixi97 – 993
Helixi109 – 12921
Beta strandi132 – 1365
Beta strandi142 – 1454
Helixi146 – 1483
Helixi151 – 17222
Beta strandi177 – 1804
Beta strandi184 – 19310
Helixi196 – 2038
Beta strandi206 – 2083
Helixi209 – 2113
Beta strandi212 – 2143
Helixi218 – 2225
Turni223 – 2253
Helixi228 – 23710
Beta strandi251 – 2544
Beta strandi262 – 2643
Helixi265 – 27814
Beta strandi284 – 2863
Helixi296 – 32227
Helixi324 – 3329
Helixi335 – 3384
Helixi347 – 3526
Helixi354 – 3563
Turni357 – 3593
Helixi362 – 3676
Helixi372 – 38312

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 2-387.

Miscellaneous databases

EvolutionaryTraceiP15587.

Family & Domainsi

Sequence similaritiesi

Belongs to the xylose isomerase family.

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.

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

P15587-1 [UniParc]FASTAAdd to Basket

« Hide

MSYQPTPEDR FTFGLWTVGW QGRDPFGDAT RPALDPVETV QRLAELGAHG    50
VTFHDDDLIP FGSSDTERES HIKRFRQALD ATGMTVPMAT TNLFTHPVFK 100
DGGFTANDRD VRRYALRKTI RNIDLAVELG AKTYVAWGGR EGAESGAAKD 150
VRVALDRMKE AFDLLGEYVT SQGYDTRFAI EPKPNEPRGD ILLPTVGHAL 200
AFIERLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK LFHIDLNGQS 250
GIKYDQDLRF GAGDLRAAFW LVDLLESAGY EGPRHFDFKP PRTEDIDGVW 300
ASAAGCMRNY LILKERAAAF RADPEVQEAL RASRLDELAQ PTAADGVQEL 350
LADRTAFEDF DVDAAAARGM AFERLDQLAM DHLLGAR 387
Length:387
Mass (Da):42,923
Last modified:January 23, 2007 - v3
Checksum:i83CCE206015B178D
GO

Sequence databases

PIRiS28986.

Cross-referencesi

Sequence databases

PIRi S28986.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MUW X-ray 0.86 A 2-387 [» ]
1S5M X-ray 0.98 A 2-387 [» ]
1S5N X-ray 0.95 A 2-387 [» ]
1XYA X-ray 1.81 A/B 2-387 [» ]
1XYB X-ray 1.96 A/B 2-387 [» ]
1XYC X-ray 2.19 A/B 2-387 [» ]
1XYL X-ray 1.80 A/B 2-387 [» ]
1XYM X-ray 1.80 A/B 2-387 [» ]
2GYI X-ray 1.60 A/B 2-387 [» ]
ProteinModelPortali P15587.
SMRi P15587. Positions 2-387.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P15587.

Family and domain databases

Gene3Di 3.20.20.150. 1 hit.
HAMAPi MF_00455. Xylose_isom_A.
InterProi IPR013022. Xyl_isomerase-like_TIM-brl.
IPR013453. XylA_actinobac.
IPR001998. Xylose_isomerase.
[Graphical view ]
Pfami PF01261. AP_endonuc_2. 1 hit.
[Graphical view ]
PRINTSi PR00688. XYLOSISMRASE.
SUPFAMi SSF51658. SSF51658. 1 hit.
TIGRFAMsi TIGR02631. xylA_Arthro. 1 hit.
PROSITEi PS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis."
    Lavie A., Allen K., Petsko G.A., Ringe D.
    Biochemistry 33:5469-5480(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS).
  2. "Crystallographic studies of the mechanism of xylose isomerase."
    Farber G.K., Glasfeld A., Tiraby G., Ringe D., Petsko G.A.
    Biochemistry 28:7289-7297(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  3. "The 3.0 A crystal structure of xylose isomerase from Streptomyces olivochromogenes."
    Farber G.K., Petsko G.A., Ringe D.
    Protein Eng. 1:459-466(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

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: July 9, 2014
This is version 99 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

External Data

Dasty 3

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