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A1SI37

- HEM12_NOCSJ

UniProt

A1SI37 - HEM12_NOCSJ

Protein

Glutamyl-tRNA reductase 2

Gene

hemA2

Organism
Nocardioides sp. (strain BAA-499 / JS614)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (06 Feb 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 sitei51 – 511NucleophileUniRule annotation
    Sitei99 – 991Important for activityUniRule annotation
    Binding sitei109 – 1091SubstrateUniRule annotation
    Binding sitei120 – 1201SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi190 – 1956NADPUniRule 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

    BioCyciNSP196162:GH4V-1991-MONOMER.
    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductase 2UniRule annotation (EC:1.2.1.70UniRule annotation)
    Short name:
    GluTR 2UniRule annotation
    Gene namesi
    Name:hemA2UniRule annotation
    Ordered Locus Names:Noca_1962
    OrganismiNocardioides sp. (strain BAA-499 / JS614)
    Taxonomic identifieri196162 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaeNocardioidaceaeNocardioides
    ProteomesiUP000000640: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 448448Glutamyl-tRNA reductase 2PRO_0000335056Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi196162.Noca_1962.

    Structurei

    3D structure databases

    ProteinModelPortaliA1SI37.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 534Substrate 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.
    HOGENOMiHOG000109649.
    KOiK02492.
    OMAiNTSRRVH.
    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.
    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.

    Sequencei

    Sequence statusi: Complete.

    A1SI37-1 [UniParc]FASTAAdd to Basket

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    MSRLTCLAFP GRSIPMAVLE RLSVAARELP ASVRALRAVP GVDQVLVLST    50
    CERTEVYAWW TDEADPAALL RALAGQRGLG PEPLLEHAVG LTGREAVQHL 100
    LRVTAGLDSF VRGESDIVGQ VRAAVQAARA EGAVGLEVQR LVDAAVNTSR 150
    RVHRSTGAGL AAGSVASTAV AAVAGLLPDG LAGRDLLVVG TGQVAVSVVA 200
    AAREAGARLT VCGRDPERAA AIAPAGARVL GLDDLPGALL DADAVVFGTS 250
    SPERLLRAGD LGPGLSEHRS GRELVVVDLC VPRNVDPDVR GVPGVRLLDL 300
    TDLRGAAVPG RRPSAPAPAA LELAEQIVAQ EVDRFLHWWV DRAAAEPVRR 350
    LRADVEACVR EEVARATRGL SPDLEPLVAE GIRRAVQHLA HGPTRRLLDA 400
    AAAGEDEVVA LLAGLFAPSA EEDQAVPAYS PQPIGNTSNA AASATPRR 448
    Length:448
    Mass (Da):46,537
    Last modified:February 6, 2007 - v1
    Checksum:iD6E37EAE8352C2A1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000509 Genomic DNA. Translation: ABL81472.1.
    RefSeqiWP_011755419.1. NC_008699.1.
    YP_923159.1. NC_008699.1.

    Genome annotation databases

    EnsemblBacteriaiABL81472; ABL81472; Noca_1962.
    GeneIDi4599868.
    KEGGinca:Noca_1962.
    PATRICi22745969. VBINocSp122728_2233.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000509 Genomic DNA. Translation: ABL81472.1 .
    RefSeqi WP_011755419.1. NC_008699.1.
    YP_923159.1. NC_008699.1.

    3D structure databases

    ProteinModelPortali A1SI37.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 196162.Noca_1962.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABL81472 ; ABL81472 ; Noca_1962 .
    GeneIDi 4599868.
    KEGGi nca:Noca_1962.
    PATRICi 22745969. VBINocSp122728_2233.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109649.
    KOi K02492.
    OMAi NTSRRVH.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci NSP196162:GH4V-1991-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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence of chromosome 1 of Nocardioides sp. JS614."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.
      , Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J., Richardson P.
      Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: BAA-499 / JS614.

    Entry informationi

    Entry nameiHEM12_NOCSJ
    AccessioniPrimary (citable) accession number: A1SI37
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 67 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