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Q4FVA9

- HEM1_PSYA2

UniProt

Q4FVA9 - HEM1_PSYA2

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Psychrobacter arcticus (strain DSM 17307 / 273-4)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (30 Aug 2005)
      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 sitei48 – 481NucleophileUniRule annotation
    Sitei130 – 1301Important for activityUniRule annotation
    Binding sitei140 – 1401SubstrateUniRule annotation
    Binding sitei151 – 1511SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi220 – 2256NADPUniRule 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

    BioCyciPARC259536:GI3A-182-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:Psyc_0176
    OrganismiPsychrobacter arcticus (strain DSM 17307 / 273-4)
    Taxonomic identifieri259536 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
    ProteomesiUP000000546: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 459459Glutamyl-tRNA reductasePRO_1000004676Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi259536.Psyc_0176.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4FVA9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni47 – 504Substrate bindingUniRule annotation
    Regioni145 – 1473Substrate 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.
    OMAiNPGEDQI.
    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. 2 hits.
    TIGRFAMsiTIGR01035. hemA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q4FVA9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLVVIGVNH KTAPVALRER LALVGDDVNI ALAQLQGFSD GSVIVSTCNR    50
    TEIYALVPES ILSPNTLLAS SALSVVESSI SLNSSTNISS TIISAHILKI 100
    KTWLADFKQL SLDEIDPYLY VHRDMHALTH WLRVAAGLDS MILGEPQILG 150
    QIKRAVHLAQ DQKALSNQLG WIVDQVFAAA KRVRNETQVG AQAVSLSYAA 200
    AKLVTQIFDD LPSRTLLVVA AGEMNRLVAM HIAGLGVGRI IICNRNPERA 250
    EALAAELRNP KRQIEVRTLQ ELPQVLAEAD IVSSCSGSMD ILIDKTMTLR 300
    ALKSRRYQPM LMIDLAVPRD IDSTVSRIDD VYLYSVDDLQ HVIAGNIEQR 350
    RQAAVDAELL VSQLVVEMDR RFQVRQVGKD IQQYRSRTHE QVDKLLQESI 400
    AKLQGDNANP EDIMIELTRR LTQNLTHAPS KLMRKAAREG DNELLDFVVS 450
    GLQDAHRHH 459
    Length:459
    Mass (Da):50,933
    Last modified:August 30, 2005 - v1
    Checksum:i9ED49868F8FC53DA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000082 Genomic DNA. Translation: AAZ18049.1.
    RefSeqiYP_263483.1. NC_007204.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ18049; AAZ18049; Psyc_0176.
    GeneIDi3514213.
    KEGGipar:Psyc_0176.
    PATRICi23054539. VBIPsyArc98534_0210.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000082 Genomic DNA. Translation: AAZ18049.1 .
    RefSeqi YP_263483.1. NC_007204.1.

    3D structure databases

    ProteinModelPortali Q4FVA9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 259536.Psyc_0176.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ18049 ; AAZ18049 ; Psyc_0176 .
    GeneIDi 3514213.
    KEGGi par:Psyc_0176.
    PATRICi 23054539. VBIPsyArc98534_0210.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci PARC259536:GI3A-182-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. 2 hits.
    TIGRFAMsi TIGR01035. hemA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
      Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
      Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 17307 / 273-4.

    Entry informationi

    Entry nameiHEM1_PSYA2
    AccessioniPrimary (citable) accession number: Q4FVA9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 76 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