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)

A4X1U1

- HEM1_SALTO

UniProt

A4X1U1 - HEM1_SALTO

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (29 May 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 sitei50 – 501NucleophileUniRule 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

    BioCyciSTRO369723:GI49-365-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:Strop_0356
    OrganismiSalinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
    Taxonomic identifieri369723 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeSalinispora
    ProteomesiUP000000235: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 455455Glutamyl-tRNA reductasePRO_1000075424Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi369723.Strop_0356.

    Structurei

    3D structure databases

    ProteinModelPortaliA4X1U1.
    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.
    HOGENOMiHOG000109649.
    KOiK02492.
    OMAiPYLYVHY.
    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.

    A4X1U1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLLVVGASY RTAPVAALER LTVAPADLSR VLTRLVAQPY VSEAVLVSTC    50
    NRVEVYAVVS GFHGGLGDIC AVLAESTGCQ PAALADHLYV HFDAAAVNHV 100
    FRVAVGLDSM VVGEAQILGQ LRDAYHWASE AETVGRLLHE LMQQALRVGK 150
    RAHSETGIDR AGQSVVTAAL GLATELLHSD LACRPALVVG AGAMGSLGVA 200
    TLARLGAGPV SVTNRGVDRA IRLAESYGAT AVPIADLTAT LSTVDIVVAA 250
    TAAPEAVLTR AVVTQALAGR NPSRGPLVLL DLAVPRDVEP GVADLPGVQV 300
    IDIDRMAALV ADGPVAADAA AVEQIVAAEV DTFLTWLRGA DVAPTVAALR 350
    GRADDVVAAE LGRLVHRRPD LTDEQRADVA RTVHRVVQRL LHQPTVRVRQ 400
    LAAEPGGDQY TALLRELFDL EVPQTSAVGT VPDVVVPDVD PQLGGDAEAP 450
    PTGGE 455
    Length:455
    Mass (Da):47,268
    Last modified:May 29, 2007 - v1
    Checksum:iE11D84256B38311B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000667 Genomic DNA. Translation: ABP52841.1.
    RefSeqiYP_001157219.1. NC_009380.1.

    Genome annotation databases

    EnsemblBacteriaiABP52841; ABP52841; Strop_0356.
    GeneIDi5056794.
    KEGGistp:Strop_0356.
    PATRICi23439601. VBISalTro43511_0367.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000667 Genomic DNA. Translation: ABP52841.1 .
    RefSeqi YP_001157219.1. NC_009380.1.

    3D structure databases

    ProteinModelPortali A4X1U1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 369723.Strop_0356.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABP52841 ; ABP52841 ; Strop_0356 .
    GeneIDi 5056794.
    KEGGi stp:Strop_0356.
    PATRICi 23439601. VBISalTro43511_0367.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci STRO369723:GI49-365-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 Salinispora tropica CNB-440."
      Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S., Udwary D.W., Richardson P.
      Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-916 / DSM 44818 / CNB-440.

    Entry informationi

    Entry nameiHEM1_SALTO
    AccessioniPrimary (citable) accession number: A4X1U1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 62 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