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P12070

- XYLA_ARTS7

UniProt

P12070 - XYLA_ARTS7

Protein

Xylose isomerase

Gene

xylA

Organism
Arthrobacter sp. (strain NRRL B3728)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    D-xylopyranose = D-xylulose.

    Cofactori

    Binds 2 magnesium ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei54 – 5411 Publication
    Active sitei57 – 5711 Publication
    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 bindingi293 – 2931Magnesium 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

    Enzyme and pathway databases

    SABIO-RKP12070.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xylose isomerase (EC:5.3.1.5)
    Gene namesi
    Name:xylA
    OrganismiArthrobacter sp. (strain NRRL B3728)
    Taxonomic identifieri1669 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 395394Xylose isomerasePRO_0000195760Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    395
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 93
    Beta strandi11 – 144
    Helixi15 – 184
    Helixi36 – 4611
    Beta strandi50 – 545
    Helixi55 – 584
    Helixi65 – 8218
    Beta strandi88 – 903
    Beta strandi94 – 963
    Helixi97 – 993
    Helixi109 – 12820
    Beta strandi132 – 1365
    Beta strandi142 – 1454
    Helixi146 – 1483
    Helixi151 – 17222
    Beta strandi177 – 1804
    Beta strandi184 – 19310
    Helixi196 – 2038
    Helixi209 – 2113
    Beta strandi212 – 2143
    Helixi218 – 2225
    Turni223 – 2253
    Helixi228 – 23710
    Beta strandi251 – 2544
    Helixi265 – 27713
    Beta strandi290 – 2923
    Helixi302 – 32827
    Helixi330 – 3389
    Turni339 – 3424
    Helixi343 – 3453
    Helixi355 – 3606
    Turni362 – 3676
    Helixi370 – 3734
    Helixi380 – 39112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DIDX-ray2.50A/B2-395[»]
    1DIEX-ray2.50A/B2-395[»]
    1XLAX-ray2.30A/B2-395[»]
    1XLBX-ray2.50A/B2-395[»]
    1XLCX-ray2.50A/B2-395[»]
    1XLDX-ray2.50A/B2-395[»]
    1XLEX-ray2.50A/B2-395[»]
    1XLFX-ray2.50A/B2-395[»]
    1XLGX-ray2.50A/B2-395[»]
    1XLHX-ray2.50A/B2-395[»]
    1XLIX-ray2.50A/B2-395[»]
    1XLJX-ray2.50A/B2-395[»]
    1XLKX-ray2.50A/B2-395[»]
    1XLLX-ray2.50A/B2-395[»]
    1XLMX-ray2.40A/B2-395[»]
    4XIAX-ray2.30A/B3-395[»]
    5XIAX-ray2.50A/B3-395[»]
    ProteinModelPortaliP12070.
    SMRiP12070. Positions 3-395.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12070.

    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.

    P12070-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVQPTPADH FTFGLWTVGW TGADPFGVAT RKNLDPVEAV HKLAELGAYG    50
    ITFHDNDLIP FDATEAEREK ILGDFNQALK DTGLKVPMVT TNLFSHPVFK 100
    DGGFTSNDRS IRRFALAKVL HNIDLAAEMG AETFVMWGGR EGSEYDGSKD 150
    LAAALDRMRE GVDTAAGYIK DKGYNLRIAL EPKPNEPRGD IFLPTVGHGL 200
    AFIEQLEHGD IVGLNPETGH EQMAGLNFTH GIAQALWAEK LFHIDLNGQR 250
    GIKYDQDLVF GHGDLTSAFF TVDLLENGFP NGGPKYTGPR HFDYKPSRTD 300
    GYDGVWDSAK ANMSMYLLLK ERALAFRADP EVQEAMKTSG VFELGETTLN 350
    AGESAADLMN DSASFAGFDA EAAAERNFAF IRLNQLAIEH LLGSR 395
    Length:395
    Mass (Da):43,292
    Last modified:January 23, 2007 - v3
    Checksum:iEA7A21FC47726369
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59466 Genomic DNA. Translation: CAA42073.1.
    PIRiS16214.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59466 Genomic DNA. Translation: CAA42073.1 .
    PIRi S16214.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DID X-ray 2.50 A/B 2-395 [» ]
    1DIE X-ray 2.50 A/B 2-395 [» ]
    1XLA X-ray 2.30 A/B 2-395 [» ]
    1XLB X-ray 2.50 A/B 2-395 [» ]
    1XLC X-ray 2.50 A/B 2-395 [» ]
    1XLD X-ray 2.50 A/B 2-395 [» ]
    1XLE X-ray 2.50 A/B 2-395 [» ]
    1XLF X-ray 2.50 A/B 2-395 [» ]
    1XLG X-ray 2.50 A/B 2-395 [» ]
    1XLH X-ray 2.50 A/B 2-395 [» ]
    1XLI X-ray 2.50 A/B 2-395 [» ]
    1XLJ X-ray 2.50 A/B 2-395 [» ]
    1XLK X-ray 2.50 A/B 2-395 [» ]
    1XLL X-ray 2.50 A/B 2-395 [» ]
    1XLM X-ray 2.40 A/B 2-395 [» ]
    4XIA X-ray 2.30 A/B 3-395 [» ]
    5XIA X-ray 2.50 A/B 3-395 [» ]
    ProteinModelPortali P12070.
    SMRi P12070. Positions 3-395.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P12070.

    Miscellaneous databases

    EvolutionaryTracei P12070.

    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. "D-xylose (D-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728. Gene cloning, sequence and expression."
      Loviny-Anderton T., Shaw P.C., Shin M.K., Hartley B.S.
      Biochem. J. 277:263-271(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "D-xylose (D-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728. Purification and properties."
      Smith C.A., Rangarajan M., Hartley B.S.
      Biochem. J. 277:255-261(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21, CHARACTERIZATION.
    3. "Mechanism for aldose-ketose interconversion by D-xylose isomerase involving ring opening followed by a 1,2-hydride shift."
      Collyer C.A., Henrick K., Blow D.M.
      J. Mol. Biol. 212:211-235(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITES HIS-54 AND ASP-57.
    4. "Structures of D-xylose isomerase from Arthrobacter strain B3728 containing the inhibitors xylitol and D-sorbitol at 2.5-A and 2.3-A resolution, respectively."
      Henrick K., Collyer C.A., Blow D.M.
      J. Mol. Biol. 208:129-157(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    5. "Comparison of backbone structures of glucose isomerase from Streptomyces and Arthrobacter."
      Henrick K., Blow D.M., Carell H.L., Glusker J.P.
      Protein Eng. 1:467-469(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPARISON OF X-RAY STRUCTURES.

    Entry informationi

    Entry nameiXYLA_ARTS7
    AccessioniPrimary (citable) accession number: P12070
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 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, 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