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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA.2 Publications

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.

Catalytic activityi

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

Enzyme regulationi

Activated by Mg2+ ions. Inhibited by metal-chelating agents such as EDTA, EGTA, 1,10-phenanthroline, 2,2'-dipyridyl, and by PtCl4 and KPdCl4 as well as Ni2+ and Co2+. Also inhibited by iodoacetamide, N-tosyl-L-phenylalanine chloromethyl ketone, and 5,5'-dithiobis(2-nitrobenzoic acid), as well as glutamycin.1 Publication

Kineticsi

  1. KM=24 µM for L-glutamyl-tRNA(Glu)1 Publication
  2. KM=39 µM for NADPH1 Publication

    Pathwayi: protoporphyrin-IX biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Glutamyl-tRNA reductase (hemA)
    2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
    This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei50Nucleophile1
    Sitei99Important for activity1
    Binding sitei109SubstrateCurated1
    Binding sitei120SubstrateBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi189 – 194NADPCurated6

    GO - Molecular functioni

    • glutamyl-tRNA reductase activity Source: EcoCyc
    • identical protein binding Source: EcoCyc
    • NADP binding Source: InterPro

    GO - Biological processi

    • protoporphyrinogen IX biosynthetic process from glutamate Source: EcoCyc

    Keywordsi

    Molecular functionOxidoreductase
    Biological processPorphyrin biosynthesis
    LigandNADP

    Enzyme and pathway databases

    BioCyciEcoCyc:GLUTRNAREDUCT-MONOMER
    MetaCyc:GLUTRNAREDUCT-MONOMER
    BRENDAi1.2.1.70 2026
    SABIO-RKP0A6X1
    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:b1210, JW1201
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10427 hemA

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi7G → D: Loss of activity. 1 Publication1
    Mutagenesisi49T → V: 10% and 5% of wild-type reductase and esterase activity, respectively. 1 Publication1
    Mutagenesisi50C → S: Loss of activity. 1 Publication1
    Mutagenesisi52R → K: 5% and 4% of wild-type reductase and esterase activity, respectively. 1 Publication1
    Mutagenesisi52R → Q: Loss of activity. 1 Publication1
    Mutagenesisi54E → K: 6% and 2% of wild-type reductase and esterase activity, respectively. 1 Publication1
    Mutagenesisi74C → S: No effect. 1 Publication1
    Mutagenesisi99H → N: 5% and 4% of wild-type reductase and esterase activity, respectively. 1 Publication1
    Mutagenesisi106G → N: Loss of activity. 1 Publication1
    Mutagenesisi109S → A: 28% and 25% of wild-type reductase and esterase activity, respectively. 1 Publication1
    Mutagenesisi114E → K: Loss of activity. 1 Publication1
    Mutagenesisi116Q → L: Loss of reductase activity. 30% of wild-type esterase activity. 1 Publication1
    Mutagenesisi145S → F: Loss of activity. 1 Publication1
    Mutagenesisi170C → S: No effect. 1 Publication1
    Mutagenesisi191G → D: Loss of reductase activity. Retains esterase activity. 1 Publication1
    Mutagenesisi314R → C: Loss of activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001140231 – 418Glutamyl-tRNA reductaseAdd BLAST418

    Proteomic databases

    PaxDbiP0A6X1
    PRIDEiP0A6X1

    Interactioni

    Subunit structurei

    Homodimer. Interacts with glutamate-1-semialdehyde 2,1-aminomutase (GSA-AM), which forms a metabolic channeling between both enzymes to protect the reactive aldehyde species GSA.2 Publications

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    DIPiDIP-9877N
    IntActiP0A6X1, 1 interactor
    STRINGi316385.ECDH10B_1263

    Structurei

    3D structure databases

    ProteinModelPortaliP0A6X1
    SMRiP0A6X1
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni49 – 52Substrate bindingCurated4
    Regioni114 – 116Substrate bindingCurated3

    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

    eggNOGiENOG4105C7E Bacteria
    COG0373 LUCA
    HOGENOMiHOG000109650
    InParanoidiP0A6X1
    KOiK02492
    OMAiFAFKCAA
    PhylomeDBiP0A6X1

    Family and domain databases

    Gene3Di3.30.460.30, 1 hit
    HAMAPiMF_00087 Glu_tRNA_reductase, 1 hit
    InterProiView protein in InterPro
    IPR000343 4pyrrol_synth_GluRdtase
    IPR015896 4pyrrol_synth_GluRdtase_dimer
    IPR015895 4pyrrol_synth_GluRdtase_N
    IPR018214 GluRdtase_CS
    IPR036453 GluRdtase_dimer_dom_sf
    IPR036343 GluRdtase_N_sf
    IPR036291 NAD(P)-bd_dom_sf
    IPR006151 Shikm_DH/Glu-tRNA_Rdtase
    PfamiView protein in Pfam
    PF00745 GlutR_dimer, 1 hit
    PF05201 GlutR_N, 1 hit
    PF01488 Shikimate_DH, 1 hit
    PIRSFiPIRSF000445 4pyrrol_synth_GluRdtase, 1 hit
    SUPFAMiSSF51735 SSF51735, 1 hit
    SSF69075 SSF69075, 1 hit
    SSF69742 SSF69742, 1 hit
    TIGRFAMsiTIGR01035 hemA, 1 hit
    PROSITEiView protein in PROSITE
    PS00747 GLUTR, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P0A6X1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTLLALGINH KTAPVSLRER VSFSPDKLDQ ALDSLLAQPM VQGGVVLSTC
    60 70 80 90 100
    NRTELYLSVE EQDNLQEALI RWLCDYHNLN EEDLRKSLYW HQDNDAVSHL
    110 120 130 140 150
    MRVASGLDSL VLGEPQILGQ VKKAFADSQK GHMKASELER MFQKSFSVAK
    160 170 180 190 200
    RVRTETDIGA SAVSVAFAAC TLARQIFESL STVTVLLVGA GETIELVARH
    210 220 230 240 250
    LREHKVQKMI IANRTRERAQ ILADEVGAEV IALSDIDERL READIIISST
    260 270 280 290 300
    ASPLPIIGKG MVERALKSRR NQPMLLVDIA VPRDVEPEVG KLANAYLYSV
    310 320 330 340 350
    DDLQSIISHN LAQRKAAAVE AETIVAQETS EFMAWLRAQS ASETIREYRS
    360 370 380 390 400
    QAEQVRDELT AKALAALEQG GDAQAIMQDL AWKLTNRLIH APTKSLQQAA
    410
    RDGDNERLNI LRDSLGLE
    Length:418
    Mass (Da):46,307
    Last modified:March 29, 2005 - v1
    Checksum:i3CEE59AC53610A88
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti151 – 168RVRTE…SVAFA → PFALKQISVPALCLSLLP in CAA35476 (PubMed:2664455).CuratedAdd BLAST18
    Sequence conflicti172L → V in CAA35476 (PubMed:2664455).Curated1
    Sequence conflicti240L → M in CAA35476 (PubMed:2664455).Curated1
    Sequence conflicti243A → R (PubMed:2684779).Curated1
    Sequence conflicti243A → R (PubMed:7543480).Curated1
    Sequence conflicti365A → R in CAA35476 (PubMed:2664455).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M30785 Genomic DNA Translation: AAA23953.1
    M25323 Genomic DNA Translation: AAA23954.1
    X17434 Genomic DNA Translation: CAA35476.1
    U18555 Genomic DNA Translation: AAC43436.1
    U00096 Genomic DNA Translation: AAC74294.1
    AP009048 Genomic DNA Translation: BAA36068.1
    D10264 Genomic DNA Translation: BAA20969.1
    PIRiA45918 BVECHA
    RefSeqiNP_415728.1, NC_000913.3
    WP_001299679.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC74294; AAC74294; b1210
    BAA36068; BAA36068; BAA36068
    GeneIDi945777
    KEGGiecj:JW1201
    eco:b1210
    PATRICifig|1411691.4.peg.1074

    Similar proteinsi

    Entry informationi

    Entry nameiHEM1_ECOLI
    AccessioniPrimary (citable) accession number: P0A6X1
    Secondary accession number(s): P13580, Q59405
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: March 28, 2018
    This is version 115 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

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