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P24300

- XYLA_STRRU

UniProt

P24300 - XYLA_STRRU

Protein

Xylose isomerase

Gene

xylA

Organism
Streptomyces rubiginosus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Involved in D-xylose catabolism.

    Catalytic activityi

    D-xylopyranose = D-xylulose.

    Cofactori

    Binds 2 magnesium ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei54 – 541
    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

    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 rubiginosus
    Taxonomic identifieri1929 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 388387Xylose isomerasePRO_0000195805Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    DIPiDIP-58982N.

    Structurei

    Secondary structure

    1
    388
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 93
    Beta strandi11 – 144
    Helixi15 – 184
    Helixi36 – 4510
    Beta strandi50 – 545
    Helixi55 – 584
    Helixi65 – 8218
    Beta strandi88 – 903
    Beta strandi94 – 963
    Helixi97 – 993
    Beta strandi103 – 1053
    Helixi109 – 12820
    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 strandi244 – 2463
    Beta strandi251 – 2544
    Helixi265 – 27814
    Beta strandi284 – 2863
    Helixi296 – 32227
    Helixi324 – 3329
    Helixi335 – 3384
    Helixi347 – 3526
    Helixi354 – 3563
    Turni357 – 3593
    Helixi362 – 3676
    Helixi372 – 38413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GW9X-ray1.55A1-387[»]
    1MNZX-ray0.99A1-388[»]
    1O1HX-ray1.40A/B2-388[»]
    1OADX-ray1.50A/B2-388[»]
    1XIBX-ray1.60A1-388[»]
    1XICX-ray1.60A1-388[»]
    1XIDX-ray1.70A1-388[»]
    1XIEX-ray1.70A1-388[»]
    1XIFX-ray1.60A1-388[»]
    1XIGX-ray1.70A1-388[»]
    1XIHX-ray1.70A1-388[»]
    1XIIX-ray1.70A1-388[»]
    1XIJX-ray1.70A1-388[»]
    1XISX-ray1.60A2-388[»]
    2G4JX-ray1.85A2-388[»]
    2GLKX-ray0.94A1-388[»]
    2GUBX-ray1.80A1-388[»]
    2GVEneutron diffraction2.20A1-388[»]
    2XISX-ray1.71A2-388[»]
    3CWHneutron diffraction2.20A1-388[»]
    3GNXX-ray2.00A/E2-388[»]
    3KBJX-ray2.00A1-388[»]
    3KBMX-ray2.00A1-388[»]
    3KBNX-ray1.53A1-388[»]
    3KBSX-ray1.80A1-388[»]
    3KBVX-ray1.80A1-388[»]
    3KBWX-ray1.60A1-388[»]
    3KCJOther1.80A1-388[»]
    3KCLOther2.00A1-388[»]
    3KCOOther1.80A1-388[»]
    3N4AX-ray1.94A2-388[»]
    3QYSX-ray1.85A1-388[»]
    3QZAOther2.00A1-388[»]
    3U3HX-ray0.97A1-388[»]
    3XISX-ray1.60A2-388[»]
    4A8IX-ray0.95A1-388[»]
    4A8LX-ray1.35A1-388[»]
    4A8NX-ray1.20A1-388[»]
    4A8RX-ray1.42A1-388[»]
    4DUOX-ray2.00A1-388[»]
    4DVOOther2.00A1-388[»]
    4E3VX-ray1.50A1-388[»]
    4J4KX-ray1.90A1-388[»]
    4LNCOther2.19A1-388[»]
    4XISX-ray1.60A2-388[»]
    8XIAX-ray1.90A1-388[»]
    9XIAX-ray1.90A1-388[»]
    ProteinModelPortaliP24300.
    SMRiP24300. Positions 1-388.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24300.

    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.

    P24300-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNYQPTPEDR FTFGLWTVGW QGRDPFGDAT RRALDPVESV RRLAELGAHG    50
    VTFHDDDLIP FGSSDSEREE HVKRFRQALD DTGMKVPMAT TNLFTHPVFK 100
    DGGFTANDRD VRRYALRKTI RNIDLAVELG AETYVAWGGR EGAESGGAKD 150
    VRDALDRMKE AFDLLGEYVT SQGYDIRFAI EPKPNEPRGD ILLPTVGHAL 200
    AFIERLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK LFHIDLNGQN 250
    GIKYDQDLRF GAGDLRAAFW LVDLLESAGY SGPRHFDFKP PRTEDFDGVW 300
    ASAAGCMRNY LILKERAAAF RADPEVQEAL RASRLDELAR PTAADGLQAL 350
    LDDRSAFEEF DVDAAAARGM AFERLDQLAM DHLLGARG 388
    Length:388
    Mass (Da):43,227
    Last modified:January 23, 2007 - v4
    Checksum:i4C675184B62C97FB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73789 Genomic DNA. Translation: AAA26838.1.
    PIRiB41339.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73789 Genomic DNA. Translation: AAA26838.1 .
    PIRi B41339.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GW9 X-ray 1.55 A 1-387 [» ]
    1MNZ X-ray 0.99 A 1-388 [» ]
    1O1H X-ray 1.40 A/B 2-388 [» ]
    1OAD X-ray 1.50 A/B 2-388 [» ]
    1XIB X-ray 1.60 A 1-388 [» ]
    1XIC X-ray 1.60 A 1-388 [» ]
    1XID X-ray 1.70 A 1-388 [» ]
    1XIE X-ray 1.70 A 1-388 [» ]
    1XIF X-ray 1.60 A 1-388 [» ]
    1XIG X-ray 1.70 A 1-388 [» ]
    1XIH X-ray 1.70 A 1-388 [» ]
    1XII X-ray 1.70 A 1-388 [» ]
    1XIJ X-ray 1.70 A 1-388 [» ]
    1XIS X-ray 1.60 A 2-388 [» ]
    2G4J X-ray 1.85 A 2-388 [» ]
    2GLK X-ray 0.94 A 1-388 [» ]
    2GUB X-ray 1.80 A 1-388 [» ]
    2GVE neutron diffraction 2.20 A 1-388 [» ]
    2XIS X-ray 1.71 A 2-388 [» ]
    3CWH neutron diffraction 2.20 A 1-388 [» ]
    3GNX X-ray 2.00 A/E 2-388 [» ]
    3KBJ X-ray 2.00 A 1-388 [» ]
    3KBM X-ray 2.00 A 1-388 [» ]
    3KBN X-ray 1.53 A 1-388 [» ]
    3KBS X-ray 1.80 A 1-388 [» ]
    3KBV X-ray 1.80 A 1-388 [» ]
    3KBW X-ray 1.60 A 1-388 [» ]
    3KCJ Other 1.80 A 1-388 [» ]
    3KCL Other 2.00 A 1-388 [» ]
    3KCO Other 1.80 A 1-388 [» ]
    3N4A X-ray 1.94 A 2-388 [» ]
    3QYS X-ray 1.85 A 1-388 [» ]
    3QZA Other 2.00 A 1-388 [» ]
    3U3H X-ray 0.97 A 1-388 [» ]
    3XIS X-ray 1.60 A 2-388 [» ]
    4A8I X-ray 0.95 A 1-388 [» ]
    4A8L X-ray 1.35 A 1-388 [» ]
    4A8N X-ray 1.20 A 1-388 [» ]
    4A8R X-ray 1.42 A 1-388 [» ]
    4DUO X-ray 2.00 A 1-388 [» ]
    4DVO Other 2.00 A 1-388 [» ]
    4E3V X-ray 1.50 A 1-388 [» ]
    4J4K X-ray 1.90 A 1-388 [» ]
    4LNC Other 2.19 A 1-388 [» ]
    4XIS X-ray 1.60 A 2-388 [» ]
    8XIA X-ray 1.90 A 1-388 [» ]
    9XIA X-ray 1.90 A 1-388 [» ]
    ProteinModelPortali P24300.
    SMRi P24300. Positions 1-388.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-58982N.

    Chemistry

    DrugBanki DB00126. Vitamin C.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P24300.

    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. "Genetic organization and regulation of the xylose degradation genes in Streptomyces rubiginosus."
      Wong H.C., Ting Y., Lin H.C., Reichert F., Myambo K., Watt K.W., Toy P.L., Drummond R.J.
      J. Bacteriol. 173:6849-6858(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "X-ray analysis of D-xylose isomerase at 1.9 A: native enzyme in complex with substrate and with a mechanism-designed inactivator."
      Carrell H.L., Glusker J.P., Burger V., Manfre F., Tritsch D., Biellmann J.-F.
      Proc. Natl. Acad. Sci. U.S.A. 86:4440-4444(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    3. "A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 A Streptomyces rubiginosus structures with xylitol and D-xylose."
      Whitlow M., Howard A.J., Finzel B.C., Poulos T.L., Winborne E., Gilliland G.L.
      Proteins 9:153-173(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

    Entry informationi

    Entry nameiXYLA_STRRU
    AccessioniPrimary (citable) accession number: P24300
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 109 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    According to the crystallographic study residue 40 could be Gln.Curated

    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