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A6UR78

- HEM1_METVS

UniProt

A6UR78 - HEM1_METVS

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanococcus vannielii (strain SB / ATCC 35089 / DSM 1224)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (21 Aug 2007)
      Previous versions | rss
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    • 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 sitei39 – 391NucleophileUniRule annotation
    Sitei74 – 741Important for activityUniRule annotation
    Binding sitei84 – 841SubstrateUniRule annotation
    Binding sitei95 – 951SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi163 – 1686NADPUniRule 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

    BioCyciMVAN406327:GI04-1127-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:Mevan_1100
    OrganismiMethanococcus vannielii (strain SB / ATCC 35089 / DSM 1224)
    Taxonomic identifieri406327 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
    ProteomesiUP000001107: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 379379Glutamyl-tRNA reductasePRO_1000004644Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi406327.Mevan_1100.

    Structurei

    3D structure databases

    ProteinModelPortaliA6UR78.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni38 – 414Substrate bindingUniRule annotation
    Regioni89 – 913Substrate 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.
    OMAiMIICEEL.

    Family and domain databases

    Gene3Di1.10.1200.70. 1 hit.
    3.40.50.720. 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.

    A6UR78-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLVIKADYKK YPLPVLESMR INEDEFYGKY DACIIVQTCN RIEAYFDEEI    50
    NDIEKIIPDF KGFDVIKGKK ATLHFLNVAC GMDSMILGEN QILGQIKSSY 100
    HKSKELKKTS KYLENLFLKA IHVGQRVRAE TKINEGGVSI GSAAVELAEM 150
    KLGLKNRNVL LIGAGEIGTL VAKALIEKHI KAVIVANRTY ERAETLAKEL 200
    KGMAVHFDKL KEAINFSDVI ICATSSPHYI LEKSDLLDVG NKIIIDIANP 250
    RDVDDSVREL ENISLYTIDD LRNISDKNLQ KRLKEVPIVE NIIEEEYGIL 300
    LKQIEKTNVE EVIKDFNTYI EDVRKKELEK AVRLCKNKSP DEIMENFSKA 350
    FVKRITHDFV SYSLSVSKED LLNSIWWKK 379
    Length:379
    Mass (Da):43,233
    Last modified:August 21, 2007 - v1
    Checksum:i4DA687CEFAEC775E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000742 Genomic DNA. Translation: ABR55000.1.
    RefSeqiWP_012065915.1. NC_009634.1.
    YP_001323612.1. NC_009634.1.

    Genome annotation databases

    EnsemblBacteriaiABR55000; ABR55000; Mevan_1100.
    GeneIDi5324539.
    KEGGimvn:Mevan_1100.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000742 Genomic DNA. Translation: ABR55000.1 .
    RefSeqi WP_012065915.1. NC_009634.1.
    YP_001323612.1. NC_009634.1.

    3D structure databases

    ProteinModelPortali A6UR78.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 406327.Mevan_1100.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABR55000 ; ABR55000 ; Mevan_1100 .
    GeneIDi 5324539.
    KEGGi mvn:Mevan_1100.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OMAi MIICEEL.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci MVAN406327:GI04-1127-MONOMER.

    Family and domain databases

    Gene3Di 1.10.1200.70. 1 hit.
    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: SB / ATCC 35089 / DSM 1224.

    Entry informationi

    Entry nameiHEM1_METVS
    AccessioniPrimary (citable) accession number: A6UR78
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: August 21, 2007
    Last modified: October 1, 2014
    This is version 55 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