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Q3JN88

- HEM1_BURP1

UniProt

Q3JN88 - HEM1_BURP1

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Burkholderia pseudomallei (strain 1710b)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 2 (20 May 2008)
      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 sitei56 – 561NucleophileUniRule annotation
    Sitei104 – 1041Important for activityUniRule annotation
    Binding sitei114 – 1141SubstrateUniRule annotation
    Binding sitei125 – 1251SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi194 – 1996NADPUniRule 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

    BioCyciBPSE320372:GBYB-3601-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:BURPS1710b_3600
    OrganismiBurkholderia pseudomallei (strain 1710b)
    Taxonomic identifieri320372 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
    ProteomesiUP000002700: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 432432Glutamyl-tRNA reductasePRO_0000335017Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi320372.BURPS1710b_3600.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3JN88.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni55 – 584Substrate bindingUniRule annotation
    Regioni119 – 1213Substrate 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.
    OrthoDBiEOG6C2WN5.

    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.

    Q3JN88-1 [UniParc]FASTAAdd to Basket

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    MQLLTIGINH HTAPVALRER VAFPLEQIKP ALSTFKSVFL GHPAPNAPEA    50
    AILSTCNRTE LYCATNDRAA RDAAIRWMSD YHRIPADELA PHVYALPQSE 100
    AVRHAFRVAS GLDSMVLGET QILGQMKNAV RTASEAGSLG TYLNQLFQRT 150
    FAVAKEVRGT TEIGAQSVSM AAAAVRLAQR IFEQVAQQRV LFIGAGEMIE 200
    LCATHFAAQG PRELVVANRT AERGAKLAER FGGRAMPLAD LPARMHEFDI 250
    IVSCTASTLP IIGLGAVERA VKARRHRPIF MVDLAVPRDI EPEVGKLKDV 300
    FLYTVDDLGA IVREGNASRQ AAVAQAEAII ETRVQNFMQW LDARSIVPVI 350
    RHMHTQADAL RRAEVERARK MLARGDDPDA VLDALSQALT NKLIHGPTSA 400
    LNRANGADRD SLIDLMRGFY QHAPRSSDTS DR 432
    Length:432
    Mass (Da):47,299
    Last modified:May 20, 2008 - v2
    Checksum:i271ACB4C096D7403
    GO

    Sequence cautioni

    The sequence ABA49373.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000124 Genomic DNA. Translation: ABA49373.1. Different initiation.
    RefSeqiYP_334965.2. NC_007434.1.

    Genome annotation databases

    EnsemblBacteriaiABA49373; ABA49373; BURPS1710b_3600.
    GeneIDi3689349.
    KEGGibpm:BURPS1710b_3600.
    PATRICi19239802. VBIBurPse115837_3745.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000124 Genomic DNA. Translation: ABA49373.1 . Different initiation.
    RefSeqi YP_334965.2. NC_007434.1.

    3D structure databases

    ProteinModelPortali Q3JN88.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 320372.BURPS1710b_3600.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABA49373 ; ABA49373 ; BURPS1710b_3600 .
    GeneIDi 3689349.
    KEGGi bpm:BURPS1710b_3600.
    PATRICi 19239802. VBIBurPse115837_3745.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109650.
    KOi K02492.
    OrthoDBi EOG6C2WN5.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci BPSE320372:GBYB-3601-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. Woods D.E., Nierman W.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 1710b.

    Entry informationi

    Entry nameiHEM1_BURP1
    AccessioniPrimary (citable) accession number: Q3JN88
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 69 of the entry and version 2 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