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O08393

- HEM1_NOSS1

UniProt

O08393 - HEM1_NOSS1

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Nostoc sp. (strain PCC 7120 / UTEX 2576)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (23 Jan 2002)
      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

    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:alr1042
    OrganismiNostoc sp. (strain PCC 7120 / UTEX 2576)
    Taxonomic identifieri103690 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
    ProteomesiUP000002483: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428Glutamyl-tRNA reductasePRO_0000113986Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi103690.alr1042.

    Structurei

    3D structure databases

    ProteinModelPortaliO08393.
    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.
    HOGENOMiHOG000109651.
    KOiK02492.
    OMAiGLSIHTT.
    OrthoDBiEOG6MWNBM.

    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.

    O08393-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIAVVGLSH KTAPVEIREK LSIPEPQTES AIAQLTSYPH IDEVAILSTC    50
    NRLEIYIVAG ETDHGIREVT QFLSEHSKLP VHSLRQHLFV LLHEDAVMHI 100
    MRVAAGLDSL VLGEGQILAQ VKNTHKLGQQ YNGIKTILNR LFKQALTAGK 150
    RVRTETSIGT GAVSISSAAV ELAQIKAENL AACRVTILGA GKMSRLLVQH 200
    LVSKGATQIS IVNRSRERAQ ELAKQFSEHP IRTHLLPEMM TVIAESHLVF 250
    TSTSATEPIL DRAKLEMVLA PNQPLMLFDI SVPRNVHTDV NELVNVQAFN 300
    VDDLKAVVAQ NYESRRKMAQ EAERLLEEEI EAFDIWWRSL ETVSTISSLR 350
    SKIETIREQE LEKALSRLGS EFGDKHQEVI EALTRGIVNK ILHDPMVQLR 400
    AQQDVEARRR CMQTLQMLFN LDVGEQFS 428
    Length:428
    Mass (Da):47,909
    Last modified:January 23, 2002 - v2
    Checksum:i06A470955F9D3C64
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331A → G in AAB58164. 1 PublicationCurated
    Sequence conflicti48 – 481S → G in AAB58164. 1 PublicationCurated
    Sequence conflicti174 – 1741Q → E in AAB58164. 1 PublicationCurated
    Sequence conflicti280 – 2801I → V in AAB58164. 1 PublicationCurated
    Sequence conflicti374 – 3807DKHQEVI → EQTSRGV in AAB58164. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U97695 Genomic DNA. Translation: AAB58164.1.
    BA000019 Genomic DNA. Translation: BAB72999.1.
    PIRiAG1936.
    RefSeqiNP_485085.1. NC_003272.1.
    WP_010995216.1. NC_003272.1.

    Genome annotation databases

    EnsemblBacteriaiBAB72999; BAB72999; BAB72999.
    GeneIDi1104636.
    KEGGiana:alr1042.
    PATRICi22771984. VBINosSp37423_1476.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U97695 Genomic DNA. Translation: AAB58164.1 .
    BA000019 Genomic DNA. Translation: BAB72999.1 .
    PIRi AG1936.
    RefSeqi NP_485085.1. NC_003272.1.
    WP_010995216.1. NC_003272.1.

    3D structure databases

    ProteinModelPortali O08393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 103690.alr1042.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB72999 ; BAB72999 ; BAB72999 .
    GeneIDi 1104636.
    KEGGi ana:alr1042.
    PATRICi 22771984. VBINosSp37423_1476.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OMAi GLSIHTT.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    UPA00668 .

    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. "Cloning and characterization of hemA, a gene encoding glutamyl tRNA reductase in the cyanobacterium Anabaena sp. strain 7120."
      Woelfle M.A., Haselkorn R.
      Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PCC 7120 / UTEX 2576.

    Entry informationi

    Entry nameiHEM1_NOSS1
    AccessioniPrimary (citable) accession number: O08393
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 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