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A9WIS2

- HEM1_CHLAA

UniProt

A9WIS2 - HEM1_CHLAA

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      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 sitei55 – 551NucleophileUniRule annotation
    Sitei103 – 1031Important for activityUniRule annotation
    Binding sitei113 – 1131SubstrateUniRule annotation
    Binding sitei124 – 1241SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi193 – 1986NADPUniRule 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

    BioCyciCAUR324602:GIXU-2637-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:Caur_2593
    OrganismiChloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
    Taxonomic identifieri324602 [NCBI]
    Taxonomic lineageiBacteriaChloroflexiChloroflexiaChloroflexalesChloroflexineaeChloroflexaceaeChloroflexus
    ProteomesiUP000002008: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 434434Glutamyl-tRNA reductasePRO_1000075402Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi324602.Caur_2593.

    Structurei

    3D structure databases

    ProteinModelPortaliA9WIS2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni54 – 574Substrate bindingUniRule annotation
    Regioni118 – 1203Substrate 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.
    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.

    A9WIS2-1 [UniParc]FASTAAdd to Basket

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    MNLFLAGLDH TTAPVEIREQ LAFSQTDLPS ALMQLTSSET GTPPLFAEAV    50
    ILSTCNRVEL YGVTNPGTTA QHVVDFLAAF HRRPAASFVH TLYFYQGEAV 100
    ARHLCATAAG LRSLVLGEAQ IQGQVRNAYE AAQRIGSVGS ILHRLFQIAL 150
    VAGKRVRHET TIGKGAASVS QAGVELARRR LGDLRGREVL LIGGGEVSEL 200
    AAQNLIANGA DRLTIVNRTS ARAAALAERY GAEMLDFGAL PQALARADIV 250
    ISSTAAPVPI IYRHHVAEAI AHKQRARACG ECDPPTMLLI DLAVPRDIAA 300
    DVAQIPGVHL FTVDDLREVV SHTIELRSAV LEIAQQIVEE QVQEFLSWMR 350
    TQEALPVLTM LRQRAEEVRN EELARALRRL HDLSPEQRAV IEGLSRSIVN 400
    KLLHLPTRCL REAAAHGQGK RYASILAELF NLEH 434
    Length:434
    Mass (Da):47,312
    Last modified:February 5, 2008 - v1
    Checksum:i1A101A099F052555
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000909 Genomic DNA. Translation: ABY35799.1.
    RefSeqiWP_012258452.1. NC_010175.1.
    YP_001636188.1. NC_010175.1.

    Genome annotation databases

    EnsemblBacteriaiABY35799; ABY35799; Caur_2593.
    GeneIDi5827062.
    KEGGicau:Caur_2593.
    PATRICi21416349. VBIChlAur28763_2921.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000909 Genomic DNA. Translation: ABY35799.1 .
    RefSeqi WP_012258452.1. NC_010175.1.
    YP_001636188.1. NC_010175.1.

    3D structure databases

    ProteinModelPortali A9WIS2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 324602.Caur_2593.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABY35799 ; ABY35799 ; Caur_2593 .
    GeneIDi 5827062.
    KEGGi cau:Caur_2593.
    PATRICi 21416349. VBIChlAur28763_2921.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    UPA00668 .
    BioCyci CAUR324602:GIXU-2637-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29366 / DSM 635 / J-10-fl.

    Entry informationi

    Entry nameiHEM1_CHLAA
    AccessioniPrimary (citable) accession number: A9WIS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 54 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