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A2CAB8

- HEM1_PROM3

UniProt

A2CAB8 - HEM1_PROM3

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Prochlorococcus marinus (strain MIT 9303)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (20 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 sitei50 – 501NucleophileUniRule annotation
    Sitei99 – 991Important for activityUniRule annotation
    Binding sitei109 – 1091SubstrateUniRule annotation
    Binding sitei120 – 1201SubstrateUniRule 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. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Chlorophyll biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciPMAR59922:GH54-1777-MONOMER.
    UniPathwayiUPA00251; UER00316.
    UPA00668.

    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:P9303_16841
    OrganismiProchlorococcus marinus (strain MIT 9303)
    Taxonomic identifieri59922 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000002274: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 436436Glutamyl-tRNA reductasePRO_1000004663Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi59922.P9303_16841.

    Structurei

    3D structure databases

    ProteinModelPortaliA2CAB8.
    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.
    HOGENOMiHOG000109651.
    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.

    A2CAB8-1 [UniParc]FASTAAdd to Basket

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    MHIAVVGLSH RTAPVEIREK LSIPEQTMET SLQTLRGNDQ VLEVSILSTC    50
    NRLEIYTLVR HPERGISAIS DFLGQHSGLA AEDLSPHLFN FHHDEAVAHL 100
    MRVAAGLDSL VLGEGQILSQ VKKMVRLGQE HKSMGPILNR LLTQAVSTGK 150
    RVRSETNLGT GAVSISSAAV ELAQLKLGQA QGEDQLMTLE SELVAVVGAG 200
    RMSRLLLQHL QAKGCSGVML LNRTRQRAED LSADFPELPV ECRPLDDLNH 250
    CLSTCSLVFT STAADDPIVD ASLLKQLKRR SFLRLIDIGV PRNIASDVVD 300
    LPGVESHDVD DLHEVVSRNQ EARQQMAKEA EVVLQEETRL FLEWWDSLEA 350
    VPTINRLRAT LEAIRAEELQ KALSRMGPDF SARERKVVEA LSKGIINKIL 400
    HTPVTQLRAP QARQERQQAL RVVACLFELD PPLEDG 436
    Length:436
    Mass (Da):48,166
    Last modified:February 20, 2007 - v1
    Checksum:iF9B7693943A4BB65
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000554 Genomic DNA. Translation: ABM78428.1.
    RefSeqiWP_011826316.1. NC_008820.1.
    YP_001017693.1. NC_008820.1.

    Genome annotation databases

    EnsemblBacteriaiABM78428; ABM78428; P9303_16841.
    GeneIDi4777406.
    KEGGipmf:P9303_16841.
    PATRICi23000852. VBIProMar17757_1736.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000554 Genomic DNA. Translation: ABM78428.1 .
    RefSeqi WP_011826316.1. NC_008820.1.
    YP_001017693.1. NC_008820.1.

    3D structure databases

    ProteinModelPortali A2CAB8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 59922.P9303_16841.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABM78428 ; ABM78428 ; P9303_16841 .
    GeneIDi 4777406.
    KEGGi pmf:P9303_16841.
    PATRICi 23000852. VBIProMar17757_1736.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    UPA00668 .
    BioCyci PMAR59922:GH54-1777-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: MIT 9303.

    Entry informationi

    Entry nameiHEM1_PROM3
    AccessioniPrimary (citable) accession number: A2CAB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: February 20, 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3