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Q9PLR2

- HEM1_CHLMU

UniProt

Q9PLR2 - HEM1_CHLMU

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlamydia muridarum (strain MoPn / Nigg)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Oct 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

    BioCyciCMUR243161:GHYU-35-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:TC_0033
    OrganismiChlamydia muridarum (strain MoPn / Nigg)
    Taxonomic identifieri243161 [NCBI]
    Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
    ProteomesiUP000000800: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 333333Glutamyl-tRNA reductasePRO_0000114005Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi243161.TC0033.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9PLR2.
    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.

    Q9PLR2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVREGEEHID EEFSLGVIGV SYRETALQQR EQVLQFLQQA QLSFYPKFPQ    50
    EEGRSVLLST CHRVELYGMA TEAIFSTLEK EIREMGAIPY FYRNQDCFSH 100
    LFCVVGGMDS LVLGETEIQG QVKRAYLQAI EEQKLAFALH FLFQKALKEG 150
    KVFRTKRSSP STEITIPAFV QHELQKQKMA RSASLLFMGY SEINRSVAYY 200
    LQKQGFSRIT FCSRQPLSLR SMDQVLREEV CFQDPYHVIF LGSSELRHAF 250
    PRSLWEGVWD FPGRLVFDFA VPRALPVQPA CRDRYIDMEQ ISDWLRQHQK 300
    EVFPLQLDSL REVGYRYWES LNRRLARRRY ASV 333
    Length:333
    Mass (Da):39,016
    Last modified:October 1, 2000 - v1
    Checksum:i81D9B761ECC8A986
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE002160 Genomic DNA. Translation: AAF38924.1.
    PIRiE81748.
    RefSeqiNP_296417.1. NC_002620.2.

    Genome annotation databases

    EnsemblBacteriaiAAF38924; AAF38924; TC_0033.
    GeneIDi1245558.
    KEGGicmu:TC_0033.
    PATRICi20371402. VBIChlMur19118_0042.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE002160 Genomic DNA. Translation: AAF38924.1 .
    PIRi E81748.
    RefSeqi NP_296417.1. NC_002620.2.

    3D structure databases

    ProteinModelPortali Q9PLR2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243161.TC0033.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF38924 ; AAF38924 ; TC_0033 .
    GeneIDi 1245558.
    KEGGi cmu:TC_0033.
    PATRICi 20371402. VBIChlMur19118_0042.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CMUR243161:GHYU-35-MONOMER.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MoPn / Nigg.

    Entry informationi

    Entry nameiHEM1_CHLMU
    AccessioniPrimary (citable) accession number: Q9PLR2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 90 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