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B2TPD9

- HEM1_CLOBB

UniProt

B2TPD9 - HEM1_CLOBB

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Clostridium botulinum (strain Eklund 17B / Type B)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (01 Jul 2008)
      Previous versions | rss
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    Functioni

    Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

    Catalytic activityi

    L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei46 – 461NucleophileUniRule annotation
    Sitei91 – 911Important for activityUniRule annotation
    Binding sitei101 – 1011SubstrateUniRule annotation
    Binding sitei112 – 1121SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi177 – 1826NADPUniRule annotation

    GO - Molecular functioni

    1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
    2. NADP binding Source: InterPro

    GO - Biological processi

    1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciCBOT508765:GJ4H-2898-MONOMER.
    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
    Short name:
    GluTRUniRule annotation
    Gene namesi
    Name:hemAUniRule annotation
    Ordered Locus Names:CLL_A2909
    OrganismiClostridium botulinum (strain Eklund 17B / Type B)
    Taxonomic identifieri935198 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000001195: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 401401Glutamyl-tRNA reductasePRO_1000093128Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi508765.CLL_A2909.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni45 – 484Substrate bindingUniRule annotation
    Regioni106 – 1083Substrate bindingUniRule annotation

    Domaini

    Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.UniRule annotation

    Sequence similaritiesi

    Belongs to the glutamyl-tRNA reductase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0373.
    HOGENOMiHOG000090159.
    KOiK02492.
    OMAiAITCGKK.
    OrthoDBiEOG6MWNBM.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00087. Glu_tRNA_reductase.
    InterProiIPR000343. 4pyrrol_synth_GluRdtase.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view]
    PfamiPF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
    SUPFAMiSSF69742. SSF69742. 1 hit.
    TIGRFAMsiTIGR01035. hemA. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B2TPD9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIAVLGIKRN TPIEIREKLT IKVNKHDEYL DKLLKYLEGV VILATCNRTE    50
    IYFNVSSINE ELLKKIFEIF NWNYSYRKYI FISEDKKACK HLFEVTCGFH 100
    SKILGEDQIL GQVKTSYFKS LNAKALNLEL QRLFQYAITC GKKFKSQSRL 150
    FEIPVSSASI VVNESINKDC KKFMVLGYGD VGRLTMKYLL AHNINEVYLA 200
    VRNKKIKDEI MDKRVNVIDF EEKNKYINDM DCVISCTSAP HIVIKKQDIN 250
    NIGSNIIIYD LAVPRDVDDD INDIDRAQVY NIDNISHIND GNKKMRFDKM 300
    DSNKFILEKY LNEYYEWKRL RSIAPFIEEL KVTSKEIYNK RITTFKNKCT 350
    DKDDVDLANR MIKSTSDYYM NRAIDIMKEE TLKGSEEECL RIIKSIFMTK 400
    K 401
    Length:401
    Mass (Da):47,009
    Last modified:July 1, 2008 - v1
    Checksum:iBA8CEE11D370581F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001056 Genomic DNA. Translation: ACD24804.1.
    RefSeqiYP_001887096.1. NC_010674.1.

    Genome annotation databases

    EnsemblBacteriaiACD24804; ACD24804; CLL_A2909.
    GeneIDi6294674.
    KEGGicbk:CLL_A2909.
    PATRICi19398632. VBICloBot123574_2819.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001056 Genomic DNA. Translation: ACD24804.1 .
    RefSeqi YP_001887096.1. NC_010674.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 508765.CLL_A2909.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACD24804 ; ACD24804 ; CLL_A2909 .
    GeneIDi 6294674.
    KEGGi cbk:CLL_A2909.
    PATRICi 19398632. VBICloBot123574_2819.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000090159.
    KOi K02492.
    OMAi AITCGKK.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CBOT508765:GJ4H-2898-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_00087. Glu_tRNA_reductase.
    InterProi IPR000343. 4pyrrol_synth_GluRdtase.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view ]
    Pfami PF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
    SUPFAMi SSF69742. SSF69742. 1 hit.
    TIGRFAMsi TIGR01035. hemA. 1 hit.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence of Clostridium botulinum strain Eklund."
      Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
      Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Eklund 17B / Type B.

    Entry informationi

    Entry nameiHEM1_CLOBB
    AccessioniPrimary (citable) accession number: B2TPD9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 47 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.UniRule annotation

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3