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O84669

- HEM1_CHLTR

UniProt

O84669 - HEM1_CHLTR

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlamydia trachomatis (strain D/UW-3/Cx)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      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 sitei61 – 611NucleophileUniRule annotation
    Sitei100 – 1001Important for activityUniRule annotation
    Binding sitei110 – 1101SubstrateUniRule annotation
    Binding sitei121 – 1211SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi189 – 1946NADPUniRule 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:CT_662
    OrganismiChlamydia trachomatis (strain D/UW-3/Cx)
    Taxonomic identifieri272561 [NCBI]
    Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
    ProteomesiUP000000431: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 335335Glutamyl-tRNA reductasePRO_0000114008Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272561.CT662.

    Structurei

    3D structure databases

    ProteinModelPortaliO84669.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni60 – 634Substrate bindingUniRule annotation
    Regioni115 – 1173Substrate 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.
    KOiK02492.
    OMAiCHRAELY.
    OrthoDBiEOG6MWNBM.

    Family and domain databases

    HAMAPiMF_00087. Glu_tRNA_reductase.
    InterProiIPR000343. 4pyrrol_synth_GluRdtase.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    [Graphical view]
    PfamiPF05201. GlutR_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF69742. SSF69742. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O84669-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVREGEERIG NRVSLGVIGV SYRETTLQQR EQVLHILQQA QGSFRPEVFQ    50
    EERDYVLLAT CHRVELYSVA PAELFDSLAQ EIELLGVSPY FYRNQDCFAH 100
    LFCVAGGLDS LVLGETEIQG QVKRAYLQAA REQKLSFALH FLFQKALKEG 150
    KVFRAKGGAP YAEITIPILV DQELRRRQID KKASLLFIGY SEINRSVAYH 200
    LQRQGFSCIT FCSRQQLPTL SMRQVVREEL CFQDPYRVVF LGSSELQYAL 250
    PHSLWESIWD IPDRIVFDFA VPRALPSHTV FPHRYVDMDQ ISDWLREHRK 300
    EVNSAHLHSL REVAYRYWNS LNQRLERRDC VGANA 335
    Length:335
    Mass (Da):38,855
    Last modified:May 30, 2000 - v2
    Checksum:iA7F799AFB3FBE61F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001273 Genomic DNA. Translation: AAC68257.2.
    PIRiH71487.
    RefSeqiNP_220181.1. NC_000117.1.

    Genome annotation databases

    EnsemblBacteriaiAAC68257; AAC68257; CT_662.
    GeneIDi884447.
    KEGGictr:CT_662.
    PATRICi20380972. VBIChlTra43535_0728.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001273 Genomic DNA. Translation: AAC68257.2 .
    PIRi H71487.
    RefSeqi NP_220181.1. NC_000117.1.

    3D structure databases

    ProteinModelPortali O84669.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272561.CT662.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC68257 ; AAC68257 ; CT_662 .
    GeneIDi 884447.
    KEGGi ctr:CT_662.
    PATRICi 20380972. VBIChlTra43535_0728.

    Phylogenomic databases

    eggNOGi COG0373.
    KOi K02492.
    OMAi CHRAELY.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .

    Family and domain databases

    HAMAPi MF_00087. Glu_tRNA_reductase.
    InterProi IPR000343. 4pyrrol_synth_GluRdtase.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    [Graphical view ]
    Pfami PF05201. GlutR_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69742. SSF69742. 1 hit.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis."
      Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.
      Science 282:754-759(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: D/UW-3/Cx.

    Entry informationi

    Entry nameiHEM1_CHLTR
    AccessioniPrimary (citable) accession number: O84669
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 91 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, 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