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P0A6X1

- HEM1_ECOLI

UniProt

P0A6X1 - HEM1_ECOLI

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (29 Mar 2005)
      Previous versions | rss
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    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

    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

    Sites

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

    Regions

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

    GO - Molecular functioni

    1. glutamyl-tRNA reductase activity Source: EcoCyc
    2. identical protein binding Source: EcoCyc
    3. NADP binding Source: InterPro
    4. protein binding Source: EcoCyc

    GO - Biological processi

    1. protoporphyrinogen IX biosynthetic process from glutamate Source: EcoCyc

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:GLUTRNAREDUCT-MONOMER.
    ECOL316407:JW1201-MONOMER.
    MetaCyc:GLUTRNAREDUCT-MONOMER.
    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10427. hemA.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71G → D: Loss of activity. 1 Publication
    Mutagenesisi49 – 491T → V: 10% and 5% of wild-type reductase and esterase activity, respectively. 1 Publication
    Mutagenesisi50 – 501C → S: Loss of activity. 1 Publication
    Mutagenesisi52 – 521R → K: 5% and 4% of wild-type reductase and esterase activity, respectively. 1 Publication
    Mutagenesisi52 – 521R → Q: Loss of activity. 1 Publication
    Mutagenesisi54 – 541E → K: 6% and 2% of wild-type reductase and esterase activity, respectively. 1 Publication
    Mutagenesisi74 – 741C → S: No effect. 1 Publication
    Mutagenesisi99 – 991H → N: 5% and 4% of wild-type reductase and esterase activity, respectively. 1 Publication
    Mutagenesisi106 – 1061G → N: Loss of activity. 1 Publication
    Mutagenesisi109 – 1091S → A: 28% and 25% of wild-type reductase and esterase activity, respectively. 1 Publication
    Mutagenesisi114 – 1141E → K: Loss of activity. 1 Publication
    Mutagenesisi116 – 1161Q → L: Loss of reductase activity. 30% of wild-type esterase activity. 1 Publication
    Mutagenesisi145 – 1451S → F: Loss of activity. 1 Publication
    Mutagenesisi170 – 1701C → S: No effect. 1 Publication
    Mutagenesisi191 – 1911G → D: Loss of reductase activity. Retains esterase activity. 1 Publication
    Mutagenesisi314 – 3141R → C: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 418418Glutamyl-tRNA reductasePRO_0000114023Add
    BLAST

    Proteomic databases

    PaxDbiP0A6X1.
    PRIDEiP0A6X1.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A6X1.

    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

    Protein-protein interaction databases

    DIPiDIP-9877N.
    IntActiP0A6X1. 1 interaction.
    STRINGi511145.b1210.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A6X1.
    SMRiP0A6X1. Positions 3-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    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.
    HOGENOMiHOG000109650.
    KOiK02492.
    OMAiLAHKLTN.
    OrthoDBiEOG6MWNBM.
    PhylomeDBiP0A6X1.

    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.

    P0A6X1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLLALGINH KTAPVSLRER VSFSPDKLDQ ALDSLLAQPM VQGGVVLSTC    50
    NRTELYLSVE EQDNLQEALI RWLCDYHNLN EEDLRKSLYW HQDNDAVSHL 100
    MRVASGLDSL VLGEPQILGQ VKKAFADSQK GHMKASELER MFQKSFSVAK 150
    RVRTETDIGA SAVSVAFAAC TLARQIFESL STVTVLLVGA GETIELVARH 200
    LREHKVQKMI IANRTRERAQ ILADEVGAEV IALSDIDERL READIIISST 250
    ASPLPIIGKG MVERALKSRR NQPMLLVDIA VPRDVEPEVG KLANAYLYSV 300
    DDLQSIISHN LAQRKAAAVE AETIVAQETS EFMAWLRAQS ASETIREYRS 350
    QAEQVRDELT AKALAALEQG GDAQAIMQDL AWKLTNRLIH APTKSLQQAA 400
    RDGDNERLNI LRDSLGLE 418
    Length:418
    Mass (Da):46,307
    Last modified:March 29, 2005 - v1
    Checksum:i3CEE59AC53610A88
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti151 – 16818RVRTE…SVAFA → PFALKQISVPALCLSLLP in CAA35476. (PubMed:2664455)CuratedAdd
    BLAST
    Sequence conflicti172 – 1721L → V in CAA35476. (PubMed:2664455)Curated
    Sequence conflicti240 – 2401L → M in CAA35476. (PubMed:2664455)Curated
    Sequence conflicti243 – 2431A → R(PubMed:2684779)Curated
    Sequence conflicti243 – 2431A → R(PubMed:7543480)Curated
    Sequence conflicti365 – 3651A → R in CAA35476. (PubMed:2664455)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_489477.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74294; AAC74294; b1210.
    BAA36068; BAA36068; BAA36068.
    GeneIDi12931822.
    945777.
    KEGGiecj:Y75_p1182.
    eco:b1210.
    PATRICi32117672. VBIEscCol129921_1258.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A45918. BVECHA.
    RefSeqi NP_415728.1. NC_000913.3.
    YP_489477.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0A6X1.
    SMRi P0A6X1. Positions 3-398.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9877N.
    IntActi P0A6X1. 1 interaction.
    STRINGi 511145.b1210.

    Proteomic databases

    PaxDbi P0A6X1.
    PRIDEi P0A6X1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74294 ; AAC74294 ; b1210 .
    BAA36068 ; BAA36068 ; BAA36068 .
    GeneIDi 12931822.
    945777.
    KEGGi ecj:Y75_p1182.
    eco:b1210.
    PATRICi 32117672. VBIEscCol129921_1258.

    Organism-specific databases

    EchoBASEi EB0422.
    EcoGenei EG10427. hemA.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109650.
    KOi K02492.
    OMAi LAHKLTN.
    OrthoDBi EOG6MWNBM.
    PhylomeDBi P0A6X1.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci EcoCyc:GLUTRNAREDUCT-MONOMER.
    ECOL316407:JW1201-MONOMER.
    MetaCyc:GLUTRNAREDUCT-MONOMER.
    SABIO-RK P0A6X1.

    Miscellaneous databases

    PROi P0A6X1.

    Gene expression databases

    Genevestigatori P0A6X1.

    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. "Cloning and structure of the hem A gene of Escherichia coli K-12."
      Li J.-M., Russell C.S., Cosloy S.D.
      Gene 82:209-217(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Isolation, nucleotide sequence, and preliminary characterization of the Escherichia coli K-12 hemA gene."
      Verkamp E., Chelm B.K.
      J. Bacteriol. 171:4728-4735(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. "Isolation and nucleotide sequence of the hemA gene of Escherichia coli K12."
      Drolet M., Peloquin L., Echelard Y., Cousineau L., Sasarman A.
      Mol. Gen. Genet. 216:347-352(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    4. "Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12."
      Strohmaier H., Remler P., Renner W., Hoegenauer G.
      J. Bacteriol. 177:4488-4500(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Cloning and characterization of genes involved in the biosynthesis of delta-aminolevulinic acid in Escherichia coli."
      Ikemi M., Murakami K., Hashimoto M., Murooka Y.
      Gene 121:127-132(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
    9. Cited for: PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, KINETIC PARAMETERS, CATALYTIC MECHANISM, MUTAGENESIS OF GLY-7; CYS-50; CYS-74; GLY-106; GLU-114; SER-145; CYS-170; GLY-191 AND ARG-314.
    10. "Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression."
      Verkamp E., Jahn M., Jahn D., Kumar A.M., Soell D.
      J. Biol. Chem. 267:8275-8280(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Complex formation between glutamyl-tRNA reductase and glutamate-1-semialdehyde 2,1-aminomutase in Escherichia coli during the initial reactions of porphyrin biosynthesis."
      Lueer C., Schauer S., Moebius K., Schulze J., Schubert W.-D., Heinz D.W., Jahn D., Moser J.
      J. Biol. Chem. 280:18568-18572(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GSA-AM.
    12. "Glutamate recognition and hydride transfer by Escherichia coli glutamyl-tRNA reductase."
      Lueer C., Schauer S., Virus S., Schubert W.-D., Heinz D.W., Moser J., Jahn D.
      FEBS J. 274:4609-4614(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-49; ARG-52; GLU-54; HIS-99; SER-109 AND GLN-116.

    Entry informationi

    Entry nameiHEM1_ECOLI
    AccessioniPrimary (citable) accession number: P0A6X1
    Secondary accession number(s): P13580, Q59405
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 93 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.

    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

    External Data

    Dasty 3