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A4SV44

- HEM1_POLSQ

UniProt

A4SV44 - HEM1_POLSQ

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Polynucleobacter necessarius subsp. asymbioticus (strain DSM 18221 / CIP 109841 / QLW-P1DMWA-1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (15 May 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 sitei56 – 561NucleophileUniRule annotation
    Sitei108 – 1081Important for activityUniRule annotation
    Binding sitei118 – 1181SubstrateUniRule annotation
    Binding sitei129 – 1291SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi198 – 2036NADPUniRule 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

    BioCyciPNEC312153:GH50-148-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:Pnuc_0137
    OrganismiPolynucleobacter necessarius subsp. asymbioticus (strain DSM 18221 / CIP 109841 / QLW-P1DMWA-1)
    Taxonomic identifieri312153 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaePolynucleobacter
    ProteomesiUP000000231: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 438438Glutamyl-tRNA reductasePRO_1000075417Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi312153.Pnuc_0137.

    Structurei

    3D structure databases

    ProteinModelPortaliA4SV44.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni55 – 584Substrate bindingUniRule annotation
    Regioni123 – 1253Substrate 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.

    A4SV44-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLLTLGINH HTAPVAIREK VAFDPEFLQE ALHDLRQHLL GANQSGLPEA    50
    TILSTCNRTE VYCAANDANA ANILHEATFD WLAKTQQLAP SSLQPHIYSL 100
    PQSDAVRHAF RVACGLDSMV IGETQILGQM KDAVRTANDA GVLGTYLNQL 150
    FQKTFAVAKE VRGSTEIGTH SISMAAASVR LSERIFEKIS EQKILFIGAG 200
    DMITLCATHF VARKPKNVAI ANRTIERGQE LADSISAQDV QAESLKLSEL 250
    PGRLHEFDII VSSTASSLPI IGLGMVESAL KQRRHKPMVM IDLAVPRDFE 300
    PEIARLDDVY LYTVDDLGVM IQTGTNLRQA AVSQAEAIIE DRVGNFMHWM 350
    QGRNAVPVIQ DIQQQGERLR QLELERAMKR LMRGDDPQEV LNAMAQGLTN 400
    KFLHGSLHAL QHSNGAERDA LIKLLPKLFA SHSKPEDH 438
    Length:438
    Mass (Da):48,347
    Last modified:May 15, 2007 - v1
    Checksum:iF959AC9ACD0203E5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000655 Genomic DNA. Translation: ABP33358.1.
    RefSeqiYP_001154922.1. NC_009379.1.

    Genome annotation databases

    EnsemblBacteriaiABP33358; ABP33358; Pnuc_0137.
    GeneIDi5052967.
    KEGGipnu:Pnuc_0137.
    PATRICi22964617. VBIPolNec12025_0141.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000655 Genomic DNA. Translation: ABP33358.1 .
    RefSeqi YP_001154922.1. NC_009379.1.

    3D structure databases

    ProteinModelPortali A4SV44.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 312153.Pnuc_0137.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABP33358 ; ABP33358 ; Pnuc_0137 .
    GeneIDi 5052967.
    KEGGi pnu:Pnuc_0137.
    PATRICi 22964617. VBIPolNec12025_0141.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci PNEC312153:GH50-148-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: DSM 18221 / CIP 109841 / QLW-P1DMWA-1.

    Entry informationi

    Entry nameiHEM1_POLSQ
    AccessioniPrimary (citable) accession number: A4SV44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 15, 2007
    Last modified: October 1, 2014
    This is version 64 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