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Q9Z7J1

- HEM1_CHLPN

UniProt

Q9Z7J1 - HEM1_CHLPN

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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 sitei51 – 511NucleophileUniRule annotation
    Sitei92 – 921Important for activityUniRule annotation
    Binding sitei102 – 1021SubstrateUniRule annotation
    Binding sitei113 – 1131SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi181 – 1866NADPUniRule 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

    BioCyciCPNE115711:GI7B-33-MONOMER.
    CPNE115713:GHEY-745-MONOMER.
    CPNE138677:GH8N-736-MONOMER.
    CPNE182082:GH4N-763-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:CPn_0714, CP_0032, CpB0741
    OrganismiChlamydia pneumoniae (Chlamydophila pneumoniae)
    Taxonomic identifieri83558 [NCBI]
    Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
    ProteomesiUP000000424: Chromosome, UP000000583: Chromosome, UP000000801: Chromosome, UP000000802: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 339339Glutamyl-tRNA reductasePRO_0000114006Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi115713.CPn0714.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z7J1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 534Substrate bindingUniRule annotation
    Regioni107 – 1093Substrate 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.
    HOGENOMiHOG000110628.
    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.

    Q9Z7J1-1 [UniParc]FASTAAdd to Basket

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    MVLGVVGISY REAALKERER AIQYLQSFEK NLFLAQRFLG KGGAFIPLLT    50
    CHRAELYYYS ESPEIAQAAL LSELTSQGIR PYRHRGLSCF THLFQVTSGI 100
    DSLIFGETEI QGQVKRAYLK GSKERELPFD LHFLFQKALK EGKEYRSRIG 150
    FPDHQVTIES VVQEILLSYD KSIYTNFLFV GYSDINRKVA AYLYQHGYHR 200
    ITFCSRQQVT APYRTLSRET LSFRQPYDVI FFGSSESASQ FSDLSCESLA 250
    SIPKRIVFDF NVPRTFLWKE TPTGFVYLDI DFISECVQKR LQCTKEGVNK 300
    AKLLLTCAAK KQWEIYEKKS SHITQRQISS PRIPSVLSY 339
    Length:339
    Mass (Da):39,104
    Last modified:May 1, 1999 - v1
    Checksum:i814E823518D6B157
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001363 Genomic DNA. Translation: AAD18853.1.
    AE002161 Genomic DNA. Translation: AAF37927.1.
    BA000008 Genomic DNA. Translation: BAA98921.1.
    AE009440 Genomic DNA. Translation: AAP98670.1.
    PIRiB72043.
    G86579.
    RefSeqiNP_224910.1. NC_000922.1.
    NP_300770.1. NC_002491.1.
    NP_444584.1. NC_002179.2.
    NP_877013.1. NC_005043.1.

    Genome annotation databases

    EnsemblBacteriaiAAD18853; AAD18853; CPn_0714.
    AAF37927; AAF37927; CP_0032.
    AAP98670; AAP98670; CpB0741.
    BAA98921; BAA98921; BAA98921.
    GeneIDi1467420.
    895228.
    919483.
    963654.
    KEGGicpa:CP0032.
    cpj:CPj0714.
    cpn:CPn0714.
    cpt:CpB0741.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001363 Genomic DNA. Translation: AAD18853.1 .
    AE002161 Genomic DNA. Translation: AAF37927.1 .
    BA000008 Genomic DNA. Translation: BAA98921.1 .
    AE009440 Genomic DNA. Translation: AAP98670.1 .
    PIRi B72043.
    G86579.
    RefSeqi NP_224910.1. NC_000922.1.
    NP_300770.1. NC_002491.1.
    NP_444584.1. NC_002179.2.
    NP_877013.1. NC_005043.1.

    3D structure databases

    ProteinModelPortali Q9Z7J1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 115713.CPn0714.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD18853 ; AAD18853 ; CPn_0714 .
    AAF37927 ; AAF37927 ; CP_0032 .
    AAP98670 ; AAP98670 ; CpB0741 .
    BAA98921 ; BAA98921 ; BAA98921 .
    GeneIDi 1467420.
    895228.
    919483.
    963654.
    KEGGi cpa:CP0032.
    cpj:CPj0714.
    cpn:CPn0714.
    cpt:CpB0741.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000110628.
    KOi K02492.
    OMAi CHRAELY.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CPNE115711:GI7B-33-MONOMER.
    CPNE115713:GHEY-745-MONOMER.
    CPNE138677:GH8N-736-MONOMER.
    CPNE182082:GH4N-763-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: CWL029.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AR39.
    3. "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
      Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
      Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: J138.
    4. "The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
      Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: TW-183.

    Entry informationi

    Entry nameiHEM1_CHLPN
    AccessioniPrimary (citable) accession number: Q9Z7J1
    Secondary accession number(s): Q9JQF2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 101 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