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P56681

- XYLA_THECA

UniProt

P56681 - XYLA_THECA

Protein

Xylose isomerase

Gene

xylA

Organism
Thermus caldophilus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (15 Jul 1999)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    D-xylopyranose = D-xylulose.

    Cofactori

    Binds 2 magnesium ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei53 – 531By similarity
    Active sitei56 – 561By similarity
    Metal bindingi180 – 1801Magnesium 1By similarity
    Metal bindingi216 – 2161Magnesium 1By similarity
    Metal bindingi216 – 2161Magnesium 2By similarity
    Metal bindingi219 – 2191Magnesium 2By similarity
    Metal bindingi244 – 2441Magnesium 1By similarity
    Metal bindingi254 – 2541Magnesium 2By similarity
    Metal bindingi256 – 2561Magnesium 2By similarity
    Metal bindingi286 – 2861Magnesium 1By 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

    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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 387387Xylose isomerasePRO_0000195811Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    387
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56681.

    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.

    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: October 1, 2014
    This is version 76 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