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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.

Catalytic activityi

D-xylopyranose = D-xylulose.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541By similarity
Active sitei57 – 571By 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

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 387386Xylose isomerasePRO_0000195803Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
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.
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

PIRi S28986.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 102 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