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Q1QED0

- HEM1_PSYCK

UniProt

Q1QED0 - HEM1_PSYCK

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Psychrobacter cryohalolentis (strain K5)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (16 May 2006)
      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
    Sitei135 – 1351Important for activityUniRule annotation
    Binding sitei145 – 1451SubstrateUniRule annotation
    Binding sitei156 – 1561SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi225 – 2306NADPUniRule 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

    BioCyciPCRY335284:GHE9-196-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:Pcryo_0189
    OrganismiPsychrobacter cryohalolentis (strain K5)
    Taxonomic identifieri335284 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
    ProteomesiUP000002425: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 464464Glutamyl-tRNA reductasePRO_1000004677Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi335284.Pcryo_0189.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1QED0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni47 – 504Substrate bindingUniRule annotation
    Regioni150 – 1523Substrate 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.
    OMAiAITCGKK.
    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.

    Q1QED0-1 [UniParc]FASTAAdd to Basket

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    MRLVVIGVNH KTAPVALRER LALVGDEVSI ALAQLQGFSD GSVIVSTCNR    50
    TEIYALVPES ILSPHTLLPN SASAVVETSV IESSMTANNS ANLSSTIISA 100
    HILKIKTWLA GFKQLSLDEI DPYLYVHRNT HALTHWLRVA AGLDSMILGE 150
    PQILGQIKRA VHMAQDQKAL SNQLGWIVDQ VFAAAKRVRN ETQVGAQAVS 200
    LSYAAAKLVT QIFDDLPSRT LLVVAAGEMN RLVATHIAGL GVGRVIICNR 250
    NPERAEALAA ELRNPNRRIE VRTLQELPQV LAEADIVSSC SGSMDILIDK 300
    TMTLRALKSR RYQPMLMIDL AVPRDIDSTV SRIDDVYLYS VDDLQHVIAG 350
    NIEQRRQAAV DAELLVSQLV VEMDRRFQVR QVGKDIQQYR TRTHEQVNKL 400
    LQASIAELHG DSANPEDIMI ELTRRLTQNL THAPSKLMRK AAREGDNELL 450
    DFVVSGLQDA HRNH 464
    Length:464
    Mass (Da):51,284
    Last modified:May 16, 2006 - v1
    Checksum:i6A7D35BF1B8B38A3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000323 Genomic DNA. Translation: ABE73973.1.
    RefSeqiWP_011512562.1. NC_007969.1.
    YP_579457.1. NC_007969.1.

    Genome annotation databases

    EnsemblBacteriaiABE73973; ABE73973; Pcryo_0189.
    GeneIDi4035669.
    KEGGipcr:Pcryo_0189.
    PATRICi23059787. VBIPsyCry128170_0241.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000323 Genomic DNA. Translation: ABE73973.1 .
    RefSeqi WP_011512562.1. NC_007969.1.
    YP_579457.1. NC_007969.1.

    3D structure databases

    ProteinModelPortali Q1QED0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 335284.Pcryo_0189.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABE73973 ; ABE73973 ; Pcryo_0189 .
    GeneIDi 4035669.
    KEGGi pcr:Pcryo_0189.
    PATRICi 23059787. VBIPsyCry128170_0241.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci PCRY335284:GHE9-196-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. "Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J.
      , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
      Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K5.

    Entry informationi

    Entry nameiHEM1_PSYCK
    AccessioniPrimary (citable) accession number: Q1QED0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 72 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