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Q7NLA8

- HEM1_GLOVI

UniProt

Q7NLA8 - HEM1_GLOVI

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Gloeobacter violaceus (strain PCC 7421)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (15 Dec 2003)
      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 sitei50 – 501NucleophileUniRule annotation
    Sitei99 – 991Important for activityUniRule annotation
    Binding sitei109 – 1091SubstrateUniRule annotation
    Binding sitei120 – 1201SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi189 – 1946NADPUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Chlorophyll biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciGVIO251221:GH9A-1228-MONOMER.
    UniPathwayiUPA00251; UER00316.
    UPA00668.

    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:glr1218
    OrganismiGloeobacter violaceus (strain PCC 7421)
    Taxonomic identifieri251221 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaGloeobacteriaGloeobacteralesGloeobacter
    ProteomesiUP000000557: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 430430Glutamyl-tRNA reductasePRO_0000114029Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi251221.gvip168.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7NLA8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni114 – 1163Substrate 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.
    OMAiLAHKLTN.
    OrthoDBiEOG6MWNBM.
    PhylomeDBiQ7NLA8.

    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.
    TIGRFAMsiTIGR01035. hemA. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7NLA8-1 [UniParc]FASTAAdd to Basket

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    MQIAVIGLSH RTAPVEIRER VSIAEGQVPE YVSRLRSCSQ VAECAILSTC    50
    NRLEIYTVLR DSEHGLREVT RFLAESKGVL LPTLQRHLFV LLHQDAVMHL 100
    MRVAAGLDSI VLGEGQILAQ VKMTQSLAQQ GKGVDRVLNQ LFKTAITAGK 150
    RVRSDTNIGT GAVSVSSAAV EMALRKKGPL HNQRCLVVGA GKMGELLVRH 200
    LLAKGARQII VLNRSLEKAA QMVEQFGLML PVATVDELTN YVPCSDLIFT 250
    CTGATEPLLT LEKMSSLRRD QSLMIFDIAV PRNVATEVDE LPNVQLFNVD 300
    HLKQVVEENR AYRQLMVTQC EEILLEQLDE FLDWWRGLEA VPTINQLRQK 350
    VETIREQELE KALSRLGTEF AEKHQGIIDS LTRAIVNKIL HDPMVQLRAQ 400
    RDIEARRRAL QTLQTLFNLE AQSNPEPPTL 430
    Length:430
    Mass (Da):48,136
    Last modified:December 15, 2003 - v1
    Checksum:i5491B16BF167B368
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000045 Genomic DNA. Translation: BAC89159.1.
    RefSeqiNP_924164.1. NC_005125.1.

    Genome annotation databases

    EnsemblBacteriaiBAC89159; BAC89159; BAC89159.
    GeneIDi2598886.
    KEGGigvi:gvip168.
    PATRICi22041849. VBIGloVio86258_1243.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000045 Genomic DNA. Translation: BAC89159.1 .
    RefSeqi NP_924164.1. NC_005125.1.

    3D structure databases

    ProteinModelPortali Q7NLA8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 251221.gvip168.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC89159 ; BAC89159 ; BAC89159 .
    GeneIDi 2598886.
    KEGGi gvi:gvip168.
    PATRICi 22041849. VBIGloVio86258_1243.

    Phylogenomic databases

    eggNOGi COG0373.
    KOi K02492.
    OMAi LAHKLTN.
    OrthoDBi EOG6MWNBM.
    PhylomeDBi Q7NLA8.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    UPA00668 .
    BioCyci GVIO251221:GH9A-1228-MONOMER.

    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.
    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: PCC 7421.

    Entry informationi

    Entry nameiHEM1_GLOVI
    AccessioniPrimary (citable) accession number: Q7NLA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 89 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