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P28462

- HEM1_CHLP8

UniProt

P28462 - HEM1_CHLP8

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327))
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 3 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).1 Publication

    Catalytic activityi

    L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei50 – 501NucleophileBy similarity
    Sitei99 – 991Important for activityBy similarity
    Binding sitei109 – 1091SubstrateBy similarity
    Binding sitei120 – 1201SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi189 – 1946NADPBy similarity

    GO - Molecular functioni

    1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
    2. NADP binding Source: InterPro

    GO - Biological processi

    1. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Chlorophyll biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciCPAR517417:GH95-766-MONOMER.
    BRENDAi1.2.1.70. 1348.
    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductase (EC:1.2.1.70)
    Short name:
    GluTR
    Gene namesi
    Name:hemA
    Ordered Locus Names:Cpar_0738
    OrganismiChlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327))
    Taxonomic identifieri517417 [NCBI]
    Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
    ProteomesiUP000008811: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 426426Glutamyl-tRNA reductasePRO_0000114009Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi517417.Cpar_0738.

    Structurei

    3D structure databases

    ProteinModelPortaliP28462.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingBy similarity
    Regioni114 – 1163Substrate bindingBy similarity

    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 By similarity.By similarity

    Sequence similaritiesi

    Belongs to the glutamyl-tRNA reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0373.
    HOGENOMiHOG000109651.
    KOiK02492.
    OMAiKSNANHV.
    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.

    P28462-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIISVGVNH KTAPIEIRER IALSEVQNKE FVTDLVSSGL ASEAMVVSTC    50
    NRTELYVVPG MPEVNCDYLK DYIISYKDAR NAVRPEHFFN RFYCGTARHL 100
    FEVSSAIDSL VLGEGQILGQ VKDAYRIAAE VGTAGILLTR LCHTAFSVAK 150
    KVKTRTKLME GAVSVSYAAV ELAQKIFSNL SMKKVLLIGA GETGELAAKH 200
    MYAKNARNIV ITNRTQSKAE ALAEELGTNR VLPYESYKEH LHEFDIIITA 250
    VSTKEYILNA AEMQQSMAKR RLKPVIILDL GLPRNVDPEV GALQNMFLKD 300
    IDALKHIIDK NLERRRAELP KVKSIIDEEL IGFGQWINTL KVRPTIVDLQ 350
    SKFIEIKEKE LERYRHKVSE EELKRMEHLT DRILKKILHH PIKMLKAPVD 400
    TADNIPSKVN LVRNIFDLEE PNQSLQ 426
    Length:426
    Mass (Da):48,142
    Last modified:October 14, 2008 - v3
    Checksum:iD169328D709EF697
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti144 – 1452TA → SP in AAC61856. (PubMed:1793335)Curated
    Sequence conflicti144 – 1452TA → SP in AAA23112. (PubMed:1793335)Curated
    Sequence conflicti191 – 22333GETGE…AEALA → VKQSWQQSTCTPRTPGTSSS PTGRNPRPRAC in AAC61856. (PubMed:1793335)CuratedAdd
    BLAST
    Sequence conflicti191 – 22333GETGE…AEALA → VKQSWQQSTCTPRTPGTSSS PTGRNPRPRAC in AAA23112. (PubMed:1793335)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96364 Genomic DNA. Translation: AAA23112.1.
    AF080069 Genomic DNA. Translation: AAC61856.1.
    CP001099 Genomic DNA. Translation: ACF11155.1.
    PIRiA48359.
    RefSeqiWP_012501988.1. NC_011027.1.
    YP_001998355.1. NC_011027.1.

    Genome annotation databases

    EnsemblBacteriaiACF11155; ACF11155; Cpar_0738.
    GeneIDi6419665.
    KEGGicpc:Cpar_0738.
    PATRICi21364734. VBIChlPar72705_0737.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96364 Genomic DNA. Translation: AAA23112.1 .
    AF080069 Genomic DNA. Translation: AAC61856.1 .
    CP001099 Genomic DNA. Translation: ACF11155.1 .
    PIRi A48359.
    RefSeqi WP_012501988.1. NC_011027.1.
    YP_001998355.1. NC_011027.1.

    3D structure databases

    ProteinModelPortali P28462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 517417.Cpar_0738.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACF11155 ; ACF11155 ; Cpar_0738 .
    GeneIDi 6419665.
    KEGGi cpc:Cpar_0738.
    PATRICi 21364734. VBIChlPar72705_0737.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OMAi KSNANHV.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CPAR517417:GH95-766-MONOMER.
    BRENDAi 1.2.1.70. 1348.

    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. "Structure and expression of the Chlorobium vibrioforme hemA gene."
      Majumdar D., Avissar Y.J., Wyche J.H., Beale S.I.
      Arch. Microbiol. 156:281-289(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Glutamyl-tRNA reductase of Chlorobium vibrioforme is a dissociable homodimer that contains one tightly bound heme per subunit."
      Srivastava A., Beale S.I.
      J. Bacteriol. 187:4444-4450(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO C-TERMINUS, FUNCTION, HEME BINDING, SUBUNIT.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NCIB 8327.

    Entry informationi

    Entry nameiHEM1_CHLP8
    AccessioniPrimary (citable) accession number: P28462
    Secondary accession number(s): B3QMK2, O87494
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 108 of the entry and version 3 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 By similarity.By similarity
    Was shown to bind heme, but the precise role of heme is unclear.

    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