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P19148

- XYLA_THETU

UniProt

P19148 - XYLA_THETU

Protein

Xylose isomerase

Gene

xylA

Organism
Thermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    D-xylopyranose = D-xylulose.

    Cofactori

    Binds 2 cobalt ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei101 – 1011
    Active sitei104 – 1041By similarity
    Metal bindingi232 – 2321Cobalt 1
    Metal bindingi268 – 2681Cobalt 1
    Metal bindingi268 – 2681Cobalt 2
    Metal bindingi271 – 2711Cobalt 2
    Metal bindingi296 – 2961Cobalt 1
    Metal bindingi307 – 3071Cobalt 2
    Metal bindingi309 – 3091Cobalt 2
    Metal bindingi339 – 3391Cobalt 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

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Carbohydrate metabolism, Pentose shunt, Xylose metabolism

    Keywords - Ligandi

    Cobalt, Metal-binding

    Enzyme and pathway databases

    SABIO-RKP19148.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xylose isomerase (EC:5.3.1.5)
    Gene namesi
    Name:xylA
    OrganismiThermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes)
    Taxonomic identifieri33950 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisThermoanaerobacterium

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi101 – 1011H → F: Abolishes activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 439439Xylose isomerasePRO_0000195817Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    439
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 266
    Helixi38 – 425
    Beta strandi44 – 474
    Helixi48 – 525
    Helixi68 – 714
    Helixi75 – 9319
    Beta strandi96 – 1016
    Helixi102 – 1054
    Helixi112 – 13019
    Beta strandi136 – 1416
    Beta strandi145 – 1473
    Helixi148 – 1503
    Helixi160 – 17920
    Beta strandi183 – 1875
    Beta strandi192 – 1954
    Helixi197 – 1993
    Helixi202 – 22221
    Beta strandi227 – 2315
    Beta strandi237 – 2448
    Helixi247 – 25610
    Turni260 – 2623
    Beta strandi263 – 2686
    Helixi269 – 2746
    Helixi279 – 28810
    Beta strandi292 – 2965
    Beta strandi304 – 3063
    Helixi315 – 32713
    Beta strandi336 – 3383
    Helixi350 – 37526
    Helixi378 – 3869
    Helixi388 – 3903
    Helixi393 – 3997
    Helixi405 – 41410
    Helixi425 – 43612

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A0CX-ray2.50A/B/C/D2-439[»]
    ProteinModelPortaliP19148.
    SMRiP19148. Positions 2-438.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19148.

    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.
    IPR013452. Xylose_isom_bac.
    IPR001998. Xylose_isomerase.
    [Graphical view]
    PfamiPF01261. AP_endonuc_2. 1 hit.
    [Graphical view]
    PRINTSiPR00688. XYLOSISMRASE.
    SUPFAMiSSF51658. SSF51658. 1 hit.
    TIGRFAMsiTIGR02630. xylose_isom_A. 1 hit.
    PROSITEiPS51415. XYLOSE_ISOMERASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19148-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKYFENVSK IKYEGPKSNN PYSFKFYNPE EVIDGKTMEE HLRFSIAYWH    50
    TFTADGTDQF GKATMQRPWN HYTDPMDIAK ARVEAAFEFF DKINAPYFCF 100
    HDRDIAPEGD TLRETNKNLD TIVAMIKDYL KTSKTKVLWG TANLFSNPRF 150
    VHGASTSCNA DVFAYSAAQV KKALEITKEL GGENYVFWGG REGYETLLNT 200
    DMEFELDNFA RFLHMAVDYA KEIGFEGQFL IEPKPKEPTK HQYDFDVANV 250
    LAFLRKYDLD KYFKVNIEAN HATLAFHDFQ HELRYARING VLGSIDANTG 300
    DMLLGWDTDQ FPTDIRMTTL AMYEVIKMGG FDKGGLNFDA KVRRASFEPE 350
    DLFLGHIAGM DAFAKGFKVA YKLVKDRVFD KFIEERYASY KDGIGADIVS 400
    GKADFRSLEK YALERSQIVN KSGRQELLES ILNQYLFAE 439
    Length:439
    Mass (Da):50,475
    Last modified:November 1, 1990 - v1
    Checksum:i55A227DBDD0EECB9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05650 Genomic DNA. Translation: AAA23285.1.
    PIRiA36598. ISCLXM.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05650 Genomic DNA. Translation: AAA23285.1 .
    PIRi A36598. ISCLXM.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A0C X-ray 2.50 A/B/C/D 2-439 [» ]
    ProteinModelPortali P19148.
    SMRi P19148. Positions 2-438.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P19148.

    Miscellaneous databases

    EvolutionaryTracei P19148.

    Family and domain databases

    Gene3Di 3.20.20.150. 1 hit.
    HAMAPi MF_00455. Xylose_isom_A.
    InterProi IPR013022. Xyl_isomerase-like_TIM-brl.
    IPR013452. Xylose_isom_bac.
    IPR001998. Xylose_isomerase.
    [Graphical view ]
    Pfami PF01261. AP_endonuc_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00688. XYLOSISMRASE.
    SUPFAMi SSF51658. SSF51658. 1 hit.
    TIGRFAMsi TIGR02630. xylose_isom_A. 1 hit.
    PROSITEi PS51415. XYLOSE_ISOMERASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Catalytic mechanism of xylose (glucose) isomerase from Clostridium thermosulfurogenes. Characterization of the structural gene and function of active site histidine."
      Lee C.Y., Bagdasarian M., Meng M.H., Zeikus J.G.
      J. Biol. Chem. 265:19082-19090(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 33743 / DSM 2229 / 4B.
    2. "Purification and characterization of thermostable glucose isomerase from Clostridium thermosulfurogenes and Thermoanaerobacter strain B6A."
      Lee C.Y., Zeikus J.G.
      Biochem. J. 273:565-571(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-7.
    3. Gallay O., Chopra R., Conti E., Brick P., Jackson R., Hartley B., Vieille C., Zeikus J.G., Blow D.
      Submitted (NOV-1997) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
      Strain: ATCC 33743 / DSM 2229 / 4B.

    Entry informationi

    Entry nameiXYLA_THETU
    AccessioniPrimary (citable) accession number: P19148
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 93 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, Direct protein sequencing

    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