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)

Q3ACT4

- HEM1_CARHZ

UniProt

Q3ACT4 - HEM1_CARHZ

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (22 Nov 2005)
      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
    Sitei99 – 991Important for activityUniRule annotation
    Binding sitei109 – 1091SubstrateUniRule annotation
    Binding sitei120 – 1201SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi189 – 1946NADPUniRule 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

    BioCyciCHYD246194:GJCN-1206-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:CHY_1207
    OrganismiCarboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
    Taxonomic identifieri246194 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeCarboxydothermus
    ProteomesiUP000002706: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 449449Glutamyl-tRNA reductasePRO_1000004606Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi246194.CHY_1207.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3ACT4.
    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.
    OMAiHEVTGEY.
    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.

    Q3ACT4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYLVVVGVNH RTAPVEVREK LSFSDHQLKD AFSALLSYPS IDGSVILSTC    50
    NRTEVYVASL DVDTGLKVVR EFLANWAGLS LSDIKNYTYN YTLYDAVHHL 100
    FRVASGLDSM ILGETQILGQ VRDAFLKASS LKASNKILNT LFQHAITVGK 150
    KVRTETGIDK NPVSISYAAV QLACSFFGSL KDKKALLIGA GKMSSLTAKH 200
    LSYYGIKEII VANRSFEKAE QFAREFNGIA VPFAKIYDIL AEVDLVISCT 250
    GAPHLIIHKE QLELVIGNRQ HPLYLIDIAV PRDIDPEIAK LPNVFLYDID 300
    KLQNVVTKNL EERKKLAEMA ENIIETELKA FIEWHSTQFV VPTIVALKKK 350
    AEEIKQKELT KALNKLGNIS EREKNIVCAL AHTILNQLLH TPIVKLKQYA 400
    LTPQGHLYTE ILQNLFDLQV EGERPKNFTH PREEMEESDE KRSYCGESR 449
    Length:449
    Mass (Da):50,498
    Last modified:November 22, 2005 - v1
    Checksum:i035209EE115F03D1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000141 Genomic DNA. Translation: ABB15744.1.
    RefSeqiYP_360050.1. NC_007503.1.

    Genome annotation databases

    EnsemblBacteriaiABB15744; ABB15744; CHY_1207.
    GeneIDi3727853.
    KEGGichy:CHY_1207.
    PATRICi21275550. VBICarHyd26463_1156.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000141 Genomic DNA. Translation: ABB15744.1 .
    RefSeqi YP_360050.1. NC_007503.1.

    3D structure databases

    ProteinModelPortali Q3ACT4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 246194.CHY_1207.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB15744 ; ABB15744 ; CHY_1207 .
    GeneIDi 3727853.
    KEGGi chy:CHY_1207.
    PATRICi 21275550. VBICarHyd26463_1156.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CHYD246194:GJCN-1206-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: Z-2901 / DSM 6008.

    Entry informationi

    Entry nameiHEM1_CARHZ
    AccessioniPrimary (citable) accession number: Q3ACT4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: November 22, 2005
    Last modified: October 1, 2014
    This is version 71 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