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A6LSY3

- HEM1_CLOB8

UniProt

A6LSY3 - HEM1_CLOB8

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium acetobutylicum)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (24 Jul 2007)
      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

    BioCyciCBEI290402:GHL5-1355-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:Cbei_1283
    OrganismiClostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium acetobutylicum)
    Taxonomic identifieri290402 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000000565: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 401401Glutamyl-tRNA reductasePRO_1000075404Add
    BLAST

    Proteomic databases

    PRIDEiA6LSY3.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi290402.Cbei_1283.

    Structurei

    3D structure databases

    ProteinModelPortaliA6LSY3.
    ModBaseiSearch...
    MobiDBiSearch...

    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.
    OMAiNISRGPR.
    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.

    A6LSY3-1 [UniParc]FASTAAdd to Basket

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    MIGLIGIRKN TPLEIREKFI VKSKKYNEYF GELLKELNEV VILATCNRTE    50
    IYFNASLNEE ELLKKIFDIF NWDYEYKKYV FITNNKDAYR HLFEVCSGFH 100
    SKILGEDQIL GQVKDAYEEA LEFKAVSLEL HRLFQEAITC GKRFRKEAKL 150
    FEIPVSSSSI VVSEAIKREC TKFMVLGYGE VGQLVMKYLL SHKIQTVYLV 200
    VRNPKIKDEI QDERVKVITF EEKNKYINSI ECIISCTSAP HPVVKTEDIS 250
    ESGSRLVIYD LSVPRDVEKE VALLSRTEVY NIDTISRIDD ENKKLRKDKM 300
    EDNRHIMNKY LKEYDEWLKL RSISHVIKNL KTVGNDVYEK RVQTFSHKSK 350
    DKNDIALAHK LIKSTSDFYI NRAIEVIKEE TLKGCGEEWI GIIEKIFMTK 400
    E 401
    Length:401
    Mass (Da):46,919
    Last modified:July 24, 2007 - v1
    Checksum:i813E3FA143D8A58A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000721 Genomic DNA. Translation: ABR33463.1.
    RefSeqiYP_001308419.1. NC_009617.1.

    Genome annotation databases

    EnsemblBacteriaiABR33463; ABR33463; Cbei_1283.
    GeneIDi5292507.
    KEGGicbe:Cbei_1283.
    PATRICi19346542. VBICloBei69853_1317.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000721 Genomic DNA. Translation: ABR33463.1 .
    RefSeqi YP_001308419.1. NC_009617.1.

    3D structure databases

    ProteinModelPortali A6LSY3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 290402.Cbei_1283.

    Proteomic databases

    PRIDEi A6LSY3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABR33463 ; ABR33463 ; Cbei_1283 .
    GeneIDi 5292507.
    KEGGi cbe:Cbei_1283.
    PATRICi 19346542. VBICloBei69853_1317.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CBEI290402:GHL5-1355-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51743 / NCIMB 8052.

    Entry informationi

    Entry nameiHEM1_CLOB8
    AccessioniPrimary (citable) accession number: A6LSY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: July 24, 2007
    Last modified: October 1, 2014
    This is version 62 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