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Q38EJ2

- Q38EJ2_TRYB2

UniProt

Q38EJ2 - Q38EJ2_TRYB2

Protein

Adenylosuccinate lyase

Gene

Tb09.160.5560

Organism
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (22 Nov 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei185 – 1851AMPImported
    Binding sitei262 – 2621AMPImported
    Metal bindingi285 – 2851MagnesiumImported
    Metal bindingi289 – 2891MagnesiumImported
    Binding sitei324 – 3241AMPImported
    Metal bindingi346 – 3461Magnesium; via carbonyl oxygenImported
    Metal bindingi348 – 3481Magnesium; via carbonyl oxygenImported
    Binding sitei350 – 3501AMPImported
    Binding sitei355 – 3551AMPImported
    Binding sitei359 – 3591AMPImported

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi29 – 302AMPImported
    Nucleotide bindingi106 – 1083AMPImported

    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. metal ion binding Source: UniProtKB-KW
    3. N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Source: UniProtKB-EC
    4. nucleotide binding Source: UniProtKB-KW

    GO - Biological processi

    1. IMP biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    LyaseUniRule annotationImported

    Keywords - Biological processi

    Purine biosynthesisUniRule annotation

    Keywords - Ligandi

    MagnesiumImported, Metal-bindingImported, Nucleotide-bindingImported

    Enzyme and pathway databases

    UniPathwayiUPA00074; UER00132.
    UPA00075; UER00336.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylosuccinate lyaseUniRule annotation (EC:4.3.2.2UniRule annotation)
    Short name:
    ASLUniRule annotation
    Alternative name(s):
    AdenylosuccinaseUniRule annotation
    Gene namesi
    ORF Names:Tb09.160.5560Imported
    OrganismiTrypanosoma brucei brucei (strain 927/4 GUTat10.1)Imported
    Taxonomic identifieri999953 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma
    ProteomesiUP000008524: Chromosome 9

    Interactioni

    Protein-protein interaction databases

    STRINGi5691.Tb09.160.5560.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4EFCX-ray2.00A/B1-471[»]
    ProteinModelPortaliQ38EJ2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0015.
    HOGENOMiHOG000252916.
    KOiK01756.
    OMAiPANYIGN.

    Family and domain databases

    Gene3Di1.10.275.10. 1 hit.
    InterProiIPR024083. Fumarase/histidase_N.
    IPR020557. Fumarate_lyase_CS.
    IPR000362. Fumarate_lyase_fam.
    IPR022761. Fumarate_lyase_N.
    IPR008948. L-Aspartase-like.
    IPR004769. Pur_lyase.
    IPR013539. PurB_C.
    [Graphical view]
    PANTHERiPTHR11444. PTHR11444. 1 hit.
    PfamiPF08328. ASL_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view]
    PRINTSiPR00149. FUMRATELYASE.
    SUPFAMiSSF48557. SSF48557. 1 hit.
    TIGRFAMsiTIGR00928. purB. 1 hit.
    PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q38EJ2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKGSPSDLN GVDYSVDNPL FALSPLDGRY KRQTKALRAF FSEYGFFRYR    50
    VLVEVEYFTA LCKDVPTIVP LRSVTDEQLQ KLRKITLDCF SVSSAEEIKR 100
    LERVTNHDIK AVEYFIKERM DTCGLSHVTE FVHFGLTSQD INNTAIPMMI 150
    RDAIVTLYLP ALDGIIGSLT SKLVDWDVPM LARTHGQPAS PTNLAKEFVV 200
    WIERLREQRR QLCEVPTTGK FGGATGNFNA HLVAYPSVNW RAFADMFLAK 250
    YLGLKRQQAT TQIENYDHLA ALCDACARLH VILIDMCRDV WQYISMGFFK 300
    QKVKEGEVGS STMPHKVNPI DFENAEGNLA LSNALLNFFA SKLPISRLQR 350
    DLTDSTVLRN LGVPIGHACV AFASISQGLE KLMISRETIS RELSSNWAVV 400
    AEGIQTVLRR ECYPKPYETL KKLTQGNTDV TEEQVRNFIN GLTDISDDVR 450
    AELLAITPFT YVGYVPRFSA K 471
    Length:471
    Mass (Da):53,120
    Last modified:November 22, 2005 - v1
    Checksum:iB3B15E435CF9DE3E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CM000207 Genomic DNA. Translation: EAN76778.1.
    RefSeqiXP_827108.1. XM_822015.1.

    Genome annotation databases

    EnsemblProtistsiEAN76778; EAN76778; Tb09.160.5560.
    GeneIDi3660448.
    KEGGitbr:Tb09.160.5560.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CM000207 Genomic DNA. Translation: EAN76778.1 .
    RefSeqi XP_827108.1. XM_822015.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4EFC X-ray 2.00 A/B 1-471 [» ]
    ProteinModelPortali Q38EJ2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5691.Tb09.160.5560.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi EAN76778 ; EAN76778 ; Tb09.160.5560 .
    GeneIDi 3660448.
    KEGGi tbr:Tb09.160.5560.

    Phylogenomic databases

    eggNOGi COG0015.
    HOGENOMi HOG000252916.
    KOi K01756.
    OMAi PANYIGN.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00132 .
    UPA00075 ; UER00336 .

    Family and domain databases

    Gene3Di 1.10.275.10. 1 hit.
    InterProi IPR024083. Fumarase/histidase_N.
    IPR020557. Fumarate_lyase_CS.
    IPR000362. Fumarate_lyase_fam.
    IPR022761. Fumarate_lyase_N.
    IPR008948. L-Aspartase-like.
    IPR004769. Pur_lyase.
    IPR013539. PurB_C.
    [Graphical view ]
    PANTHERi PTHR11444. PTHR11444. 1 hit.
    Pfami PF08328. ASL_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00149. FUMRATELYASE.
    SUPFAMi SSF48557. SSF48557. 1 hit.
    TIGRFAMsi TIGR00928. purB. 1 hit.
    PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome of the African trypanosome Trypanosoma brucei."
      Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H., Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U., Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B., Alsmark U.C.M.
      , Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F., Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C., Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A., Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D., Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D., Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S., Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S., Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G., Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A., Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M., Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S., Walker D., Wanless D., Wang S., White B., White O., Whitehead S., Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E., Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E., Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.
      Science 309:416-422(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 927/4 GUTat10.1Imported.
    2. "Crystal Structure of Adenylosuccinate Lyase from Trypanosoma Brucei, Tb427tmp.160.5560."
      Wernimont A.K., Loppnau P., Osman K.T., Arrowsmith C.H., Edwards A.M., Bountra C., Robinson D.A., Wyatt P.G., Gilbert I.H., Hui R., Lin Y.H.
      Submitted (MAR-2012) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH AMP AND MAGNESIUM.

    Entry informationi

    Entry nameiQ38EJ2_TRYB2
    AccessioniPrimary (citable) accession number: Q38EJ2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 22, 2005
    Last sequence update: November 22, 2005
    Last modified: October 1, 2014
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported, Complete proteome, Reference proteomeImported

    External Data

    Dasty 3