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)

Q6LNB3

- HEM1_PHOPR

UniProt

Q6LNB3 - HEM1_PHOPR

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Photobacterium profundum (Photobacterium sp. (strain SS9))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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
    Sitei97 – 971Important for activityUniRule annotation
    Binding sitei107 – 1071SubstrateUniRule annotation
    Binding sitei118 – 1181SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi187 – 1926NADPUniRule 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

    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:PBPRA2846
    OrganismiPhotobacterium profundum (Photobacterium sp. (strain SS9))
    Taxonomic identifieri74109 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium
    ProteomesiUP000000593: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 420420Glutamyl-tRNA reductasePRO_0000114054Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi298386.PBPRA2846.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6LNB3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni112 – 1143Substrate 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.
    OMAiLAHKLTN.
    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.

    Q6LNB3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLLALGINH NTASVDLREK VAFSPDKLKE ALQQLESHPE VTSSIIVSTC    50
    NRTEVYCDVT HSGPGVMIDW LAKFHRLSAE EILPSLYFHE EQAAARHLMR 100
    VACGLDSLVL GEPQILGQVK QSYYSSQEYD AIHGTLEKLF HKTFTVAKRV 150
    RTETDIGGNA VSVAYAACTL AKQIFESLSD TTVLLVGAGE TIELVSRHLV 200
    EQGCNKLIVA NRTKERAANL AEEFGAEVIG LPEIPEHLHR ADIVISSTAS 250
    PLPIVGKGMV EKAIKARRHQ PMLFVDIAVP RDVEAEVGDL NDVYLYTVDD 300
    LHSIIEKNRE QRKVAAIQAE AIISEESAAF MSWLRSLEAV DSIRQYRCFA 350
    DDIKNDMLSR SLQAIANGVA PEKVLVELSN KLTNKLIHAP TRAMQQAAHN 400
    GEPEKLSVIR ETLGLDSIKD 420
    Length:420
    Mass (Da):46,335
    Last modified:July 5, 2004 - v1
    Checksum:iCC8F8571ACED3576
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR378672 Genomic DNA. Translation: CAG21213.1.
    RefSeqiYP_131015.1. NC_006370.1.

    Genome annotation databases

    EnsemblBacteriaiCAG21213; CAG21213; PBPRA2846.
    GeneIDi3122003.
    KEGGippr:PBPRA2846.
    PATRICi22936722. VBIPhoPro109272_3039.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR378672 Genomic DNA. Translation: CAG21213.1 .
    RefSeqi YP_131015.1. NC_006370.1.

    3D structure databases

    ProteinModelPortali Q6LNB3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 298386.PBPRA2846.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAG21213 ; CAG21213 ; PBPRA2846 .
    GeneIDi 3122003.
    KEGGi ppr:PBPRA2846.
    PATRICi 22936722. VBIPhoPro109272_3039.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .

    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: SS9.

    Entry informationi

    Entry nameiHEM1_PHOPR
    AccessioniPrimary (citable) accession number: Q6LNB3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 77 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