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P42804

- HEM11_ARATH

UniProt

P42804 - HEM11_ARATH

Protein

Glutamyl-tRNA reductase 1, chloroplastic

Gene

HEMA1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (03 Apr 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). Probably involved in the tetrapyrrole synthesis required for the chlorophyll biosynthesis.2 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Negatively regulated by FLU and heme.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei144 – 1441NucleophileBy similarity
    Sitei193 – 1931Important for activityBy similarity
    Binding sitei203 – 2031SubstrateBy similarity
    Binding sitei214 – 2141SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi285 – 2906NADPBy similarity

    GO - Molecular functioni

    1. glutamyl-tRNA reductase activity Source: TAIR
    2. NADP binding Source: InterPro
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. chlorophyll biosynthetic process Source: TAIR
    2. heme biosynthetic process Source: TAIR
    3. 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

    BioCyciARA:AT1G58290-MONOMER.
    MetaCyc:AT1G58290-MONOMER.
    UniPathwayiUPA00251; UER00316.
    UPA00668.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductase 1, chloroplastic (EC:1.2.1.70)
    Short name:
    GluTR
    Gene namesi
    Name:HEMA1
    Synonyms:HEMA
    Ordered Locus Names:At1g58290
    ORF Names:F19C14.9
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G58290.

    Subcellular locationi

    Plastidchloroplast membrane 2 Publications

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. chloroplast membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Membrane, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6464ChloroplastSequence AnalysisAdd
    BLAST
    Chaini65 – 543479Glutamyl-tRNA reductase 1, chloroplasticPRO_0000013307Add
    BLAST

    Proteomic databases

    PaxDbiP42804.
    PRIDEiP42804.

    Expressioni

    Tissue specificityi

    Strongly expressed in photosynthetic tissues. Detected in all tissues tested.3 Publications

    Inductioni

    Circadian-regulation. Up-regulated by light.4 Publications

    Gene expression databases

    ArrayExpressiP42804.
    GenevestigatoriP42804.

    Interactioni

    Subunit structurei

    Part of the FLU-containing chloroplast membrane complex composed of FLU, CRD1, PORB, PORC, CHLP and HEMA1. Interacts (via C-terminus) with FLU, only in the absence of light.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FLUQ940U63EBI-2319900,EBI-2319882

    Protein-protein interaction databases

    BioGridi27423. 4 interactions.
    IntActiP42804. 4 interactions.
    MINTiMINT-8300920.
    STRINGi3702.AT1G58290.1-P.

    Structurei

    Secondary structure

    1
    543
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi96 – 1038
    Turni104 – 1063
    Helixi109 – 1157
    Helixi119 – 1213
    Helixi122 – 13110
    Beta strandi135 – 1439
    Beta strandi146 – 15510
    Helixi156 – 17116
    Helixi175 – 1817
    Beta strandi183 – 1864
    Helixi188 – 19811
    Beta strandi202 – 2054
    Beta strandi207 – 2093
    Helixi211 – 22212
    Helixi230 – 24819
    Turni252 – 2554
    Helixi259 – 27012
    Beta strandi273 – 2764
    Beta strandi281 – 2844
    Helixi288 – 29912
    Beta strandi304 – 3107
    Helixi312 – 32110
    Beta strandi325 – 3317
    Helixi332 – 3343
    Helixi335 – 3406
    Beta strandi343 – 3475
    Helixi358 – 3625
    Helixi369 – 3713
    Beta strandi375 – 3795
    Helixi388 – 3925
    Beta strandi396 – 4005
    Helixi401 – 4077
    Turni414 – 4163
    Helixi417 – 43923
    Helixi440 – 4423
    Helixi443 – 46422
    Helixi480 – 49213
    Turni493 – 4975
    Helixi513 – 52311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4N7RX-ray2.80A/B73-543[»]
    ProteinModelPortaliP42804.
    SMRiP42804. Positions 97-468.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni143 – 1464Substrate bindingBy similarity
    Regioni208 – 2103Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi23 – 3311Poly-SerAdd
    BLAST
    Compositional biasi305 – 3084Poly-Val

    Domaini

    The N-terminus (65-92) is required for heme inhibition, but not for activity.1 Publication

    Sequence similaritiesi

    Belongs to the glutamyl-tRNA reductase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0373.
    HOGENOMiHOG000109651.
    InParanoidiP42804.
    KOiK02492.
    OMAiLAHKLTN.
    PhylomeDBiP42804.

    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]
    SUPFAMiSSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    TIGRFAMsiTIGR01035. hemA. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P42804-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVSSAFVGC PKLETLLNHH NLSPSSSSSS SVSQTPLGLN GVRVLPKNNR    50
    TRRGLIQKAR CELSASSDSA SNAASISALE QLKNSAADRY TKERSSIVVI 100
    GLSIHTAPVE MREKLAIPEA EWPRAIAELC GLNHIEEAAV LSTCNRMEIY 150
    VLALSQHRGV KEVTEWMSKT SGIPVSEICQ HRFLLYNKDA TQHIFEVSAG 200
    LDSLVLGEGQ ILAQVKQVVK VGQGVNGFGR NISGLFKHAI TVGKRVRTET 250
    NIASGAVSVS SAAVELALMK LPQSSNVSAR MCVIGAGKMG KLVIKHLMAK 300
    GCTKVVVVNR SEERVSAIRE EMPGIEIIYR PLDEMLACAS EADVVFTSTA 350
    SETPLFLKEH VENLPQASPE VGGLRHFVDI SVPRNVGSCV GEVETARVYN 400
    VDDLKEVVAA NKEDRMRKAM EAQTIITEES TQFEAWRDSL ETVPTIKKLR 450
    AYAERIRVAE LEKCMSKMGD DINKKTTRAV DDLSRGIVNR FLHGPMQHLR 500
    CDGSDSRTLS ETLENMHALN RMYGLEKDIL EEKLKAMAEQ QQK 543
    Length:543
    Mass (Da):59,515
    Last modified:April 3, 2002 - v2
    Checksum:i04A095FEC96CC014
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti62 – 621E → V in AAA19118. (PubMed:7908550)Curated
    Sequence conflicti169 – 1691K → N in AAA19118. (PubMed:7908550)Curated
    Sequence conflicti291 – 2911K → L in AAA19118. (PubMed:7908550)Curated
    Sequence conflicti443 – 4431V → G in BAE98482. 1 PublicationCurated
    Sequence conflicti542 – 5421Q → H in AAA19118. (PubMed:7908550)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03774 Genomic DNA. Translation: AAA19118.1.
    AC008051 Genomic DNA. Translation: AAF82258.1.
    CP002684 Genomic DNA. Translation: AEE33532.1.
    AY072223 mRNA. Translation: AAL60044.1.
    AY096600 mRNA. Translation: AAM20250.1.
    AK226332 mRNA. Translation: BAE98482.1.
    PIRiE96616.
    RefSeqiNP_176125.1. NM_104609.3.
    UniGeneiAt.241.

    Genome annotation databases

    EnsemblPlantsiAT1G58290.1; AT1G58290.1; AT1G58290.
    GeneIDi842198.
    KEGGiath:AT1G58290.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03774 Genomic DNA. Translation: AAA19118.1 .
    AC008051 Genomic DNA. Translation: AAF82258.1 .
    CP002684 Genomic DNA. Translation: AEE33532.1 .
    AY072223 mRNA. Translation: AAL60044.1 .
    AY096600 mRNA. Translation: AAM20250.1 .
    AK226332 mRNA. Translation: BAE98482.1 .
    PIRi E96616.
    RefSeqi NP_176125.1. NM_104609.3.
    UniGenei At.241.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4N7R X-ray 2.80 A/B 73-543 [» ]
    ProteinModelPortali P42804.
    SMRi P42804. Positions 97-468.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 27423. 4 interactions.
    IntActi P42804. 4 interactions.
    MINTi MINT-8300920.
    STRINGi 3702.AT1G58290.1-P.

    Proteomic databases

    PaxDbi P42804.
    PRIDEi P42804.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G58290.1 ; AT1G58290.1 ; AT1G58290 .
    GeneIDi 842198.
    KEGGi ath:AT1G58290.

    Organism-specific databases

    TAIRi AT1G58290.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    InParanoidi P42804.
    KOi K02492.
    OMAi LAHKLTN.
    PhylomeDBi P42804.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    UPA00668 .
    BioCyci ARA:AT1G58290-MONOMER.
    MetaCyc:AT1G58290-MONOMER.

    Gene expression databases

    ArrayExpressi P42804.
    Genevestigatori P42804.

    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 ]
    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. "Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis."
      Ilag L.L., Kumar A.M., Soell D.
      Plant Cell 6:265-275(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
      Strain: cv. Columbia.
      Tissue: Leaf.
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "Regulation of HEMA1 expression by phytochrome and a plastid signal during de-etiolation in Arabidopsis thaliana."
      McCormac A.C., Fischer A., Kumar A.M., Soll D., Terry M.J.
      Plant J. 25:549-561(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY LIGHT, TISSUE SPECIFICITY.
    7. "Divergent regulation of the HEMA gene family encoding glutamyl-tRNA reductase in Arabidopsis thaliana: expression of HEMA2 is regulated by sugars, but is independent of light and plastid signalling."
      Ujwal M.L., McCormac A.C., Goulding A., Kumar A.M., Soell D., Terry M.J.
      Plant Mol. Biol. 50:83-91(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION BY LIGHT.
    8. "Concurrent interactions of heme and FLU with Glu tRNA reductase (HEMA1), the target of metabolic feedback inhibition of tetrapyrrole biosynthesis, in dark- and light-grown Arabidopsis plants."
      Goslings D., Meskauskiene R., Kim C., Lee K.P., Nater M., Apel K.
      Plant J. 40:957-967(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLU, ENZYME REGULATION, DOMAIN.
      Strain: cv. Landsberg erecta.
    9. Cited for: INDUCTION BY LIGHT.
    10. "FLU, a negative feedback regulator of tetrapyrrole biosynthesis, is physically linked to the final steps of the Mg(++)-branch of this pathway."
      Kauss D., Bischof S., Steiner S., Apel K., Meskauskiene R.
      FEBS Lett. 586:211-216(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE FLU-CONTAINING CHLOROPLAST MEMBRANE COMPLEX, ENZYME REGULATION.

    Entry informationi

    Entry nameiHEM11_ARATH
    AccessioniPrimary (citable) accession number: P42804
    Secondary accession number(s): Q0WWL6, Q9LQB9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: April 3, 2002
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3