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Q97B68

- HEM1_THEVO

UniProt

Q97B68 - HEM1_THEVO

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Oct 2001)
      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 sitei49 – 491NucleophileUniRule annotation
    Sitei79 – 791Important for activityUniRule annotation
    Binding sitei89 – 891SubstrateUniRule annotation
    Binding sitei100 – 1001SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi165 – 1706NADPUniRule 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

    BioCyciTVOL273116:GC31-614-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:TV0590
    ORF Names:TVG0579613
    OrganismiThermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
    Taxonomic identifieri273116 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
    ProteomesiUP000001017: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 409409Glutamyl-tRNA reductasePRO_0000114113Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi273116.TVN0590.

    Structurei

    Secondary structure

    1
    409
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi145 – 15612
    Beta strandi160 – 1645
    Helixi168 – 1736
    Helixi174 – 1763
    Turni179 – 1813
    Beta strandi183 – 1897
    Helixi191 – 20111
    Beta strandi204 – 2074
    Helixi211 – 2166
    Beta strandi219 – 2235
    Helixi234 – 2363
    Beta strandi242 – 2454
    Beta strandi258 – 2603
    Helixi261 – 27414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OJ0X-ray1.65A141-281[»]
    ProteinModelPortaliQ97B68.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ97B68.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni48 – 514Substrate bindingUniRule annotation
    Regioni94 – 963Substrate 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.
    KOiK02492.
    OMAiEHMIEDE.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00087. Glu_tRNA_reductase.
    InterProiIPR000343. 4pyrrol_synth_GluRdtase.
    IPR015896. 4pyrrol_synth_GluRdtase_dimer.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view]
    PfamiPF00745. GlutR_dimer. 1 hit.
    PF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
    SUPFAMiSSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q97B68-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLMNIVTLIS WDFKRNNESF QRAIINGYDY WSRILDDHGV EKYVILLTCN    50
    RVELYYRGDP FDVQEKGYNI ISDDMAINHL FHVAAGLDSM SIGENEVLKQ 100
    VKQAYEKSSS MGKSDKFLSL IFQRAISVGK LVRSKTGIGK GKVSIPSIVY 150
    DIVRKNGGNK ILLVGNGMLA SEIAPYFSYP QYKVTVAGRN IDHVRAFAEK 200
    YEYEYVLIND IDSLIKNNDV IITATSSKTP IVEERSLMPG KLFIDLGNPP 250
    NIERGNNVIT LDEIYEISKK NEMLREEKIN QAEILIENEM KATMNKIKDL 300
    MIDDIFSQFY RFASVVQTME IQKFRKMHPE VNENDLEALA HSIINKILNV 350
    PVTTLKAVSR SQGNSDFNRL FESFSSNFND IVSAALQSYE GLRDTQSLRD 400
    RTRQLLQKS 409
    Length:409
    Mass (Da):46,691
    Last modified:October 1, 2001 - v1
    Checksum:i8CF23510B233D830
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000011 Genomic DNA. Translation: BAB59732.1.
    RefSeqiNP_111109.1. NC_002689.2.

    Genome annotation databases

    EnsemblBacteriaiBAB59732; BAB59732; BAB59732.
    GeneIDi1441696.
    KEGGitvo:TVN0590.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000011 Genomic DNA. Translation: BAB59732.1 .
    RefSeqi NP_111109.1. NC_002689.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3OJ0 X-ray 1.65 A 141-281 [» ]
    ProteinModelPortali Q97B68.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273116.TVN0590.

    Protocols and materials databases

    DNASUi 1441696.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB59732 ; BAB59732 ; BAB59732 .
    GeneIDi 1441696.
    KEGGi tvo:TVN0590.

    Phylogenomic databases

    eggNOGi COG0373.
    KOi K02492.
    OMAi EHMIEDE.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci TVOL273116:GC31-614-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q97B68.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_00087. Glu_tRNA_reductase.
    InterProi IPR000343. 4pyrrol_synth_GluRdtase.
    IPR015896. 4pyrrol_synth_GluRdtase_dimer.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view ]
    Pfami PF00745. GlutR_dimer. 1 hit.
    PF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
    SUPFAMi SSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1.

    Entry informationi

    Entry nameiHEM1_THEVO
    AccessioniPrimary (citable) accession number: Q97B68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2002
    Last sequence update: October 1, 2001
    Last modified: October 1, 2014
    This is version 91 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

    3D-structure, Complete 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