Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A7HA35

- HEM11_ANADF

UniProt

A7HA35 - HEM11_ANADF

Protein

Glutamyl-tRNA reductase 1

Gene

hemA1

Organism
Anaeromyxobacter sp. (strain Fw109-5)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (11 Sep 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei53 – 531NucleophileUniRule annotation
    Sitei94 – 941Important for activityUniRule annotation
    Binding sitei104 – 1041SubstrateUniRule annotation
    Binding sitei115 – 1151SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi184 – 1896NADPUniRule 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

    BioCyciASP404589:GHMT-1383-MONOMER.
    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductase 1UniRule annotation (EC:1.2.1.70UniRule annotation)
    Short name:
    GluTR 1UniRule annotation
    Gene namesi
    Name:hemA1UniRule annotation
    Ordered Locus Names:Anae109_1374
    OrganismiAnaeromyxobacter sp. (strain Fw109-5)
    Taxonomic identifieri404589 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeAnaeromyxobacteraceaeAnaeromyxobacter
    ProteomesiUP000006382: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 440440Glutamyl-tRNA reductase 1PRO_0000335007Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi404589.Anae109_1374.

    Structurei

    3D structure databases

    ProteinModelPortaliA7HA35.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 554Substrate bindingUniRule annotation
    Regioni109 – 1113Substrate 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.
    OMAiHEVTGEY.
    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.

    A7HA35-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNGKEIFLVG LSHKSAPIEV RERVALTGDL LKAALCELRA AESVAEAFVV    50
    STCNRVEVYV QADGIEPARR FFTERAPDAD EHLYAKIGVE AIRHLFRVSA 100
    SLDSMVVGEQ QILGQVKEAY GLASAAEAAG PFMSRLCNRA FATAKRVRTE 150
    TDIGRGATSM SQVAVELVEK IFGDLKGRAI LLVGAGKMGA LSAKALAVLG 200
    ADRILVTNRS PERGLALAEQ VGGAFRGWDE LPRLLVEADV VIVSTGAPTY 250
    VVTRDLVQQA MKARRRRSLC LIDLAVPRNV DPACADLGEV FAYDVDDMEK 300
    VVTATQEARR GEALRAEAIV EAEVMAFAKE RDARAALPVL AQLRRHAEQI 350
    ARAEAERTLS HLGPKLDEKG KKSVEAMAQA IVNKLLHGPT ARLKAAAATG 400
    DGDLPGAAAE LFGIDNDPAR PEGAPAQPAE GRAAASSERS 440
    Length:440
    Mass (Da):46,929
    Last modified:September 11, 2007 - v1
    Checksum:i941DD32337F8E19C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000769 Genomic DNA. Translation: ABS25581.1.
    RefSeqiWP_011985687.1. NC_009675.1.
    YP_001378565.1. NC_009675.1.

    Genome annotation databases

    EnsemblBacteriaiABS25581; ABS25581; Anae109_1374.
    GeneIDi5375324.
    KEGGiafw:Anae109_1374.
    PATRICi20927931. VBIAnaSp113478_1445.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000769 Genomic DNA. Translation: ABS25581.1 .
    RefSeqi WP_011985687.1. NC_009675.1.
    YP_001378565.1. NC_009675.1.

    3D structure databases

    ProteinModelPortali A7HA35.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 404589.Anae109_1374.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABS25581 ; ABS25581 ; Anae109_1374 .
    GeneIDi 5375324.
    KEGGi afw:Anae109_1374.
    PATRICi 20927931. VBIAnaSp113478_1445.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci ASP404589:GHMT-1383-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: Fw109-5.

    Entry informationi

    Entry nameiHEM11_ANADF
    AccessioniPrimary (citable) accession number: A7HA35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 60 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