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)

A7MY81

- HEM1_VIBCB

UniProt

A7MY81 - HEM1_VIBCB

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Vibrio campbellii (strain ATCC BAA-1116 / BB120)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (02 Oct 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
    Sitei97 – 971Important for activityUniRule annotation
    Binding sitei107 – 1071SubstrateUniRule annotation
    Binding sitei118 – 1181SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi187 – 1926NADPUniRule 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

    BioCyciVHAR338187:GJCH-1239-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:VIBHAR_01249
    OrganismiVibrio campbellii (strain ATCC BAA-1116 / BB120)
    Taxonomic identifieri338187 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000008152: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 418418Glutamyl-tRNA reductasePRO_1000004722Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi338187.VIBHAR_01249.

    Structurei

    3D structure databases

    ProteinModelPortaliA7MY81.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni112 – 1143Substrate 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.
    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.

    A7MY81-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLLAIGINH NTASVDLREK VAFGPDKLGP ALEQLREHEA VNGSVIVSTC    50
    NRTEVYCDVK QGARNKLIDW LAQFHQVNQE DLMPSLYVHE EQAAIKHLMR 100
    VSCGLDSLVL GEPQILGQVK QAFSDSRDHQ AVDTSIDKLF QKTFSVAKRV 150
    RTETDIGGNA VSVAYAACTL AKHIFESLSD STVLLVGAGE TIELVAKHLA 200
    SNGCTKMIVA NRTRERALGL GEQFGAEVIS LNEIPDHLPR ADIVISSTAS 250
    PLPIIGKGMV ETALKKRRHQ PMLLVDIAVP RDVEAQVGEL SDAYLYSVDD 300
    LQSIIDSNIE QRKVEAIQAE AIVSEESAAF MTWLRSLQAV DSIRDYRKSA 350
    NEIREDLLSK SLQSLATGAD PEKVLRELSN KLTNKLIHAP TRALQSAAEQ 400
    GEPAKLTVIR QTLGLDDL 418
    Length:418
    Mass (Da):45,727
    Last modified:October 2, 2007 - v1
    Checksum:i22650B7BBBA818CF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000789 Genomic DNA. Translation: ABU70228.1.
    RefSeqiYP_001444455.1. NC_009783.1.
    YP_008526124.1. NC_022269.1.

    Genome annotation databases

    EnsemblBacteriaiABU70228; ABU70228; VIBHAR_01249.
    GeneIDi16815523.
    5556175.
    KEGGivca:M892_06765.
    vha:VIBHAR_01249.
    PATRICi20129328. VBIVibHar24526_1214.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000789 Genomic DNA. Translation: ABU70228.1 .
    RefSeqi YP_001444455.1. NC_009783.1.
    YP_008526124.1. NC_022269.1.

    3D structure databases

    ProteinModelPortali A7MY81.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 338187.VIBHAR_01249.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABU70228 ; ABU70228 ; VIBHAR_01249 .
    GeneIDi 16815523.
    5556175.
    KEGGi vca:M892_06765.
    vha:VIBHAR_01249.
    PATRICi 20129328. VBIVibHar24526_1214.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci VHAR338187:GJCH-1239-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: ATCC BAA-1116 / BB120.

    Entry informationi

    Entry nameiHEM1_VIBCB
    AccessioniPrimary (citable) accession number: A7MY81
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: October 2, 2007
    Last modified: October 1, 2014
    This is version 56 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