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Q5L782

- HEM1_CHLAB

UniProt

Q5L782 - HEM1_CHLAB

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlamydophila abortus (strain DSM 27085 / S26/3)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (21 Jun 2005)
      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

    BioCyciCABO218497:GJB0-30-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:CAB028
    OrganismiChlamydophila abortus (strain DSM 27085 / S26/3)
    Taxonomic identifieri218497 [NCBI]
    Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila
    ProteomesiUP000001012: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 338338Glutamyl-tRNA reductasePRO_1000093121Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi218497.CAB028.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5L782.
    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.

    Q5L782-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLGVVGISY REAALKEREA VINILKDFEA NSFFSQHFFG DDGSFVLLLT    50
    CHRAEIYYFS KSNRHIQSKL LSRISSLGAR PYCYQGLACF THLFTVTSGM 100
    DSLISGETEI QGQVKRAYIK AKTDRDLPFA LHFLFQKALK EGKDFRSQVS 150
    LSHPVVTIES VVEETLDLHG KSTKDKLLFI GYSEINRKIA KGLSAKGYRN 200
    LIFCSRKNIS IPYDTVARSQ LSFREPYDVI FFGSSESAKD FSGLSLESLA 250
    SIPSRVIFDF NVPRTFTLAE SPKDIICLDM DFISERVQKK LQISKQCTNK 300
    EKPFLALAAR KQWEVYEKKS SHIPSSQVRA SRPKLLIL 338
    Length:338
    Mass (Da):38,300
    Last modified:June 21, 2005 - v1
    Checksum:i12DEC577C95B9289
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR848038 Genomic DNA. Translation: CAH63486.1.
    RefSeqiYP_219460.1. NC_004552.2.

    Genome annotation databases

    EnsemblBacteriaiCAH63486; CAH63486; CAB028.
    GeneIDi3337916.
    KEGGicab:CAB028.
    PATRICi20201396. VBIChlAbo21869_0029.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR848038 Genomic DNA. Translation: CAH63486.1 .
    RefSeqi YP_219460.1. NC_004552.2.

    3D structure databases

    ProteinModelPortali Q5L782.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 218497.CAB028.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAH63486 ; CAH63486 ; CAB028 .
    GeneIDi 3337916.
    KEGGi cab:CAB028.
    PATRICi 20201396. VBIChlAbo21869_0029.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CABO218497:GJB0-30-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: DSM 27085 / S26/3.

    Entry informationi

    Entry nameiHEM1_CHLAB
    AccessioniPrimary (citable) accession number: Q5L782
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: June 21, 2005
    Last modified: October 1, 2014
    This is version 62 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