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P56681

- XYLA_THECA

UniProt

P56681 - XYLA_THECA

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Protein
Xylose isomerase
Gene
xylA
Organism
Thermus caldophilus
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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 sitei53 – 531 By similarity
Active sitei56 – 561 By similarity
Metal bindingi180 – 1801Magnesium 1 By similarity
Metal bindingi216 – 2161Magnesium 1 By similarity
Metal bindingi216 – 2161Magnesium 2 By similarity
Metal bindingi219 – 2191Magnesium 2 By similarity
Metal bindingi244 – 2441Magnesium 1 By similarity
Metal bindingi254 – 2541Magnesium 2 By similarity
Metal bindingi256 – 2561Magnesium 2 By similarity
Metal bindingi286 – 2861Magnesium 1 By similarity

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
OrganismiThermus caldophilus
Taxonomic identifieri272 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

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
Chaini1 – 387387Xylose isomeraseUniRule annotation
PRO_0000195811Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83
Beta strandi10 – 134
Helixi14 – 174
Helixi35 – 4511
Beta strandi48 – 536
Helixi54 – 574
Helixi64 – 8118
Beta strandi87 – 893
Beta strandi93 – 953
Helixi96 – 983
Helixi108 – 12720
Beta strandi132 – 1354
Beta strandi141 – 1433
Helixi145 – 1473
Helixi149 – 1513
Helixi153 – 17119
Beta strandi176 – 1794
Beta strandi183 – 19210
Helixi195 – 2028
Beta strandi205 – 2073
Helixi208 – 2103
Beta strandi211 – 2133
Helixi217 – 2215
Turni222 – 2243
Helixi227 – 23711
Beta strandi243 – 2453
Beta strandi250 – 2534
Helixi264 – 27613
Beta strandi283 – 2853
Helixi295 – 32127
Helixi323 – 33210
Turni337 – 3393
Helixi340 – 3423
Beta strandi343 – 3453
Helixi348 – 3569
Helixi361 – 3655
Helixi371 – 38212

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXCX-ray2.30A/B/C/D1-387[»]
ProteinModelPortaliP56681.
SMRiP56681. Positions 1-387.

Miscellaneous databases

EvolutionaryTraceiP56681.

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.

P56681-1 [UniParc]FASTAAdd to Basket

« Hide

MYEPKPEHRF TFGLWTVGNV GRDPFGDAVR ERLDPVYVGH KLAELGVHGV    50
NLHDEDLIPR GTPPAERDQI VRRFKRALDE TGLKVPMVTG NLFSDPGFKD 100
GGFTSRDPWV RAYAFRKSLE TMDLGAELGA EIYVVWPGRE GAEVEATGKA 150
RKVWDWVREP LNFMAAYAED QGYGYRFALE PKPNEPRGDI YFATVGSMLA 200
LIHTLERPER FGLNPEFAHE TMAGLNFVHA VAQALDAGKL LHIDLNGQRM 250
NRFDQDLRFG SENLKAAFLL VDLLESSGYQ GPRHFDAHAL RTEDEEGVWA 300
FARGCMRTYL ILKERAEAFR EDPEVKELLA AYYQEDPAAL PLMDPYSHEK 350
AEALKRAELP LEAKRHRGYA LERLDQLAVE YLLGVRG 387
Length:387
Mass (Da):43,860
Last modified:July 15, 1999 - v1
Checksum:i28FB6568BA758065
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BXC X-ray 2.30 A/B/C/D 1-387 [» ]
ProteinModelPortali P56681.
SMRi P56681. Positions 1-387.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P56681.

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. "A thermostable xylose isomerase from Thermus caldophilus: biochemical characterization, crystallization and preliminary X-ray analysis."
    Chang C., Song H.K., Park B.C., Lee D.-S., Suh S.W.
    Acta Crystallogr. D 55:294-296(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION, CHARACTERIZATION.
    Strain: GK24.
  2. "Crystal structures of thermostable xylose isomerases from Thermus caldophilus and Thermus thermophilus: possible structural determinants of thermostability."
    Chang C., Park B.C., Lee D.-S., Suh S.W.
    J. Mol. Biol. 288:623-634(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    Strain: GK24.

Entry informationi

Entry nameiXYLA_THECA
AccessioniPrimary (citable) accession number: P56681
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: February 19, 2014
This is version 75 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

External Data

Dasty 3

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