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Q9X0I0

- PUR8_THEMA

UniProt

Q9X0I0 - PUR8_THEMA

Protein

Adenylosuccinate lyase

Gene

purB

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.
    (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei95 – 951SubstrateBy similarity
    Active sitei141 – 1411Proton acceptor1 Publication
    Active sitei141 – 1411Proton donor/acceptorBy similarity
    Binding sitei212 – 2121SubstrateBy similarity
    Active sitei262 – 2621Proton donor/acceptorBy similarity
    Binding sitei301 – 3011SubstrateBy similarity
    Binding sitei306 – 3061SubstrateBy similarity
    Binding sitei310 – 3101SubstrateBy similarity

    GO - Molecular functioni

    1. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity Source: UniProtKB-EC
    2. N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Source: UniProtKB-EC

    GO - Biological processi

    1. 'de novo' AMP biosynthetic process Source: UniProtKB-UniPathway
    2. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Purine biosynthesis

    Enzyme and pathway databases

    UniPathwayiUPA00074; UER00132.
    UPA00075; UER00336.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylosuccinate lyase (EC:4.3.2.2)
    Short name:
    ASL
    Alternative name(s):
    Adenylosuccinase
    Short name:
    ASase
    Gene namesi
    Name:purB
    Ordered Locus Names:TM_1095
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 431431Adenylosuccinate lyasePRO_0000137886Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site.1 Publication

    Protein-protein interaction databases

    STRINGi243274.TM1095.

    Structurei

    Secondary structure

    1
    431
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 53
    Helixi10 – 134
    Helixi16 – 3621
    Helixi44 – 518
    Helixi56 – 6611
    Helixi69 – 8113
    Helixi82 – 876
    Turni88 – 914
    Helixi94 – 13037
    Turni131 – 1333
    Beta strandi135 – 1406
    Beta strandi143 – 1497
    Helixi150 – 17425
    Beta strandi188 – 1903
    Helixi192 – 20110
    Beta strandi211 – 2133
    Helixi217 – 24327
    Turni246 – 2483
    Beta strandi250 – 2523
    Helixi272 – 28615
    Helixi288 – 2936
    Helixi304 – 33330
    Helixi338 – 3458
    Turni346 – 3505
    Helixi351 – 3533
    Helixi354 – 36310
    Helixi368 – 38316
    Beta strandi385 – 3873
    Helixi389 – 3946
    Helixi397 – 4004
    Helixi405 – 4106
    Helixi415 – 4184
    Helixi421 – 4266

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C3CX-ray1.80A/B2-430[»]
    1C3UX-ray2.30A/B1-431[»]
    ProteinModelPortaliQ9X0I0.
    SMRiQ9X0I0. Positions 2-430.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9X0I0.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni4 – 52Substrate bindingBy similarity
    Regioni67 – 693Substrate bindingBy similarity
    Regioni68 – 692Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0015.
    KOiK01756.
    OMAiRNMGSTF.
    OrthoDBiEOG686NDB.

    Family and domain databases

    Gene3Di1.10.275.10. 1 hit.
    InterProiIPR019468. AdenyloSucc_lyase_C.
    IPR024083. Fumarase/histidase_N.
    IPR020557. Fumarate_lyase_CS.
    IPR000362. Fumarate_lyase_fam.
    IPR022761. Fumarate_lyase_N.
    IPR008948. L-Aspartase-like.
    IPR004769. Pur_lyase.
    [Graphical view]
    PANTHERiPTHR11444. PTHR11444. 1 hit.
    PfamiPF10397. ADSL_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view]
    PRINTSiPR00149. FUMRATELYASE.
    SMARTiSM00998. ADSL_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48557. SSF48557. 1 hit.
    TIGRFAMsiTIGR00928. purB. 1 hit.
    PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9X0I0-1 [UniParc]FASTAAdd to Basket

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    MVERYSLSPM KDLWTEEAKY RRWLEVELAV TRAYEELGMI PKGVTERIRN    50
    NAKIDVELFK KIEEKTNHDV VAFVEGIGSM IGEDSRFFHY GLTSSDVLDT 100
    ANSLALVEAG KILLESLKEF CDVLWEVANR YKHTPTIGRT HGVHAEPTSF 150
    GLKVLGWYSE MKRNVQRLER AIEEVSYGKI SGAVGNYANV PPEVEEKALS 200
    YLGLKPEPVS TQVVPRDRHA FYLSTLAIVA AGIERIAVEI RHLQRTEVLE 250
    VEEPFRKGQR GSSAMPHKKN PITCERLTGL SRMMRAYVDP SLENIALWHE 300
    RDISHSSVER YVFPDATQTL YYMIVTATNV VRNMKVNEER MKKNIDLTKG 350
    LVFSQRVLLK LIEKGLTRKE AYDIVQRNAL KTWNSEKHFL EYLLEDEEVK 400
    KLVTKEELEE LFDISYYLKH VDHIFERFEK E 431
    Length:431
    Mass (Da):49,873
    Last modified:November 1, 1999 - v1
    Checksum:iD3ACB25D87582869
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36171.1.
    PIRiA72294.
    RefSeqiNP_228901.1. NC_000853.1.
    WP_004080360.1. NC_023151.1.
    YP_007977450.1. NC_021214.1.
    YP_008991807.1. NC_023151.1.

    Genome annotation databases

    EnsemblBacteriaiAAD36171; AAD36171; TM_1095.
    GeneIDi898670.
    KEGGitma:TM1095.
    tmi:THEMA_08870.
    tmm:Tmari_1101.
    PATRICi23937125. VBITheMar51294_1111.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36171.1 .
    PIRi A72294.
    RefSeqi NP_228901.1. NC_000853.1.
    WP_004080360.1. NC_023151.1.
    YP_007977450.1. NC_021214.1.
    YP_008991807.1. NC_023151.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C3C X-ray 1.80 A/B 2-430 [» ]
    1C3U X-ray 2.30 A/B 1-431 [» ]
    ProteinModelPortali Q9X0I0.
    SMRi Q9X0I0. Positions 2-430.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243274.TM1095.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD36171 ; AAD36171 ; TM_1095 .
    GeneIDi 898670.
    KEGGi tma:TM1095.
    tmi:THEMA_08870.
    tmm:Tmari_1101.
    PATRICi 23937125. VBITheMar51294_1111.

    Phylogenomic databases

    eggNOGi COG0015.
    KOi K01756.
    OMAi RNMGSTF.
    OrthoDBi EOG686NDB.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00132 .
    UPA00075 ; UER00336 .

    Miscellaneous databases

    EvolutionaryTracei Q9X0I0.

    Family and domain databases

    Gene3Di 1.10.275.10. 1 hit.
    InterProi IPR019468. AdenyloSucc_lyase_C.
    IPR024083. Fumarase/histidase_N.
    IPR020557. Fumarate_lyase_CS.
    IPR000362. Fumarate_lyase_fam.
    IPR022761. Fumarate_lyase_N.
    IPR008948. L-Aspartase-like.
    IPR004769. Pur_lyase.
    [Graphical view ]
    PANTHERi PTHR11444. PTHR11444. 1 hit.
    Pfami PF10397. ADSL_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00149. FUMRATELYASE.
    SMARTi SM00998. ADSL_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48557. SSF48557. 1 hit.
    TIGRFAMsi TIGR00928. purB. 1 hit.
    PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    2. "The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway."
      Toth E.A., Yeates T.O.
      Structure 8:163-174(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT, ACTIVE SITE.

    Entry informationi

    Entry nameiPUR8_THEMA
    AccessioniPrimary (citable) accession number: Q9X0I0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 113 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, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3