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A4G1N3

- HEM1_HERAR

UniProt

A4G1N3 - HEM1_HERAR

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Herminiimonas arsenicoxydans
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (17 Apr 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 sitei57 – 571NucleophileUniRule annotation
    Sitei109 – 1091Important for activityUniRule annotation
    Binding sitei119 – 1191SubstrateUniRule annotation
    Binding sitei130 – 1301SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi199 – 2046NADPUniRule 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

    BioCyciHARS204773:GJCA-181-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:HEAR0186
    OrganismiHerminiimonas arsenicoxydans
    Taxonomic identifieri204773 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceaeHerminiimonas
    ProteomesiUP000006697: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 429429Glutamyl-tRNA reductasePRO_0000335046Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi204773.HEAR0186.

    Structurei

    3D structure databases

    ProteinModelPortaliA4G1N3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni56 – 594Substrate bindingUniRule annotation
    Regioni124 – 1263Substrate 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.
    HOGENOMiHOG000109650.
    KOiK02492.
    OMAiLAHKLTN.
    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.

    A4G1N3-1 [UniParc]FASTAAdd to Basket

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    MQLLAVGLNH TTAPVSLREK VAFPADQLGQ AVASARVWYG RSDSKTYSDE    50
    AAILSTCNRT ELYAASHQPG GVNEAIDLTA HFLADYHKLP YSELRPYLYA 100
    LPQDNAVRHA FRVASGLDSM VLGEPQILGQ MKDAVRQAEA AGGLGTYLHQ 150
    MFQRTFAVAK EVRSNTEIGA HSVSMAAASV RLSQRIFDTI SEQNVLFIGA 200
    GEMIELCATH FAAQNPKSLT IANRTLERGE TLAHRFNGRA IRLADLPDQL 250
    ASYDIVISST ASSLPIIGLG MVERAIKARR HKPMFMVDLA VPRDIETEIG 300
    RLDDVFLYTV DDLGTFVQTG LENRQAAVTQ AEAIIETRVQ SFMHWIDARA 350
    VVPVIQDLHE SSEMMRMIEL ERARKLLAKG EDIDAVLEAL SKGLTAKFLH 400
    GPQQALNNAQ GDERTRLAAL LPQLFRTKR 429
    Length:429
    Mass (Da):47,289
    Last modified:April 17, 2007 - v1
    Checksum:iB6C8D0E7E83455F1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU207211 Genomic DNA. Translation: CAL60420.1.
    RefSeqiWP_011869769.1. NC_009138.1.
    YP_001098549.1. NC_009138.1.

    Genome annotation databases

    EnsemblBacteriaiCAL60420; CAL60420; HEAR0186.
    GeneIDi4932130.
    KEGGihar:HEAR0186.
    PATRICi22110578. VBIHerArs17568_0189.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU207211 Genomic DNA. Translation: CAL60420.1 .
    RefSeqi WP_011869769.1. NC_009138.1.
    YP_001098549.1. NC_009138.1.

    3D structure databases

    ProteinModelPortali A4G1N3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 204773.HEAR0186.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAL60420 ; CAL60420 ; HEAR0186 .
    GeneIDi 4932130.
    KEGGi har:HEAR0186.
    PATRICi 22110578. VBIHerArs17568_0189.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109650.
    KOi K02492.
    OMAi LAHKLTN.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci HARS204773:GJCA-181-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: ULPAs1.

    Entry informationi

    Entry nameiHEM1_HERAR
    AccessioniPrimary (citable) accession number: A4G1N3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 65 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