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P49294

- HEM12_ARATH

UniProt

P49294 - HEM12_ARATH

Protein

Glutamyl-tRNA reductase 2, chloroplastic

Gene

HEMA2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (24 Jul 2007)
      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 wound-induced supply of heme to defensive hemoproteins outside plastids.3 Publications

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei135 – 1351NucleophileBy similarity
    Sitei184 – 1841Important for activityBy similarity
    Binding sitei194 – 1941SubstrateBy similarity
    Binding sitei205 – 2051SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi277 – 2826NADPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. chlorophyll biosynthetic process Source: UniProtKB-UniPathway
    2. heme biosynthetic process Source: TAIR
    3. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
    4. response to oxidative stress Source: TAIR
    5. tetrapyrrole biosynthetic process Source: TAIR

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Chlorophyll biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciARA:AT1G09940-MONOMER.
    MetaCyc:AT1G09940-MONOMER.
    UniPathwayiUPA00251; UER00316.
    UPA00668.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductase 2, chloroplastic (EC:1.2.1.70)
    Short name:
    GluTR
    Gene namesi
    Name:HEMA2
    Ordered Locus Names:At1g09940
    ORF Names:F21M12.33
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G09940.

    Subcellular locationi

    Plastidchloroplast By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype, but decreased heme content in roots.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6464ChloroplastSequence AnalysisAdd
    BLAST
    Chaini65 – 530466Glutamyl-tRNA reductase 2, chloroplasticPRO_0000013308Add
    BLAST

    Proteomic databases

    PRIDEiP49294.

    Expressioni

    Tissue specificityi

    Expressed in roots and flowers. Detected in leaves, hypocotyls and cotyledons.4 Publications

    Inductioni

    Not regulated by light. Up-regulated localy by wounding and reactive oxygen species. Not regulated by methyl jasmonate.3 Publications

    Gene expression databases

    GenevestigatoriP49294.

    Structurei

    3D structure databases

    ProteinModelPortaliP49294.
    SMRiP49294. Positions 88-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni134 – 1374Substrate bindingBy similarity
    Regioni199 – 2013Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glutamyl-tRNA reductase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0373.
    HOGENOMiHOG000109651.
    InParanoidiP49294.
    KOiK02492.
    OMAiAITCGKK.
    PhylomeDBiP49294.

    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.

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

    P49294-1 [UniParc]FASTAAdd to Basket

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    MAVSSAFVVT PKLEKLLANH HNPTYSSSPA PLDVIGIRAL PMNNRNKRGL    50
    IQRARCEISP SNKAASISAL EQLKTSAIDR YTKERSSIVV IGLSIHTAPV 100
    EMREKLAIPE AEWPRAIAEL CGLNHIEEAA VLSTCNRMEI YVLALSQHRG 150
    VKEVTEWMSK TSGIPVSEIC QHRFLLYNKD VTQHIFEVSA GLDSLVLGEG 200
    QILAQVKQVV KVGQGVNGFG RNISGLFKHA ITVGKRVRTE TNIAAGAVSV 250
    SSAAVELALM KLPESSHASS ARMLVVGAGK MGKLVIKHLV AKGCTKMVVV 300
    NRSEEKVAAV RNEMPPGVEI IYKPLDEMLS CAAEADVVFT STASETPLFL 350
    KEQVETLPPV RDARLFVDIS VPRNVGSCVA EIDGTRVFNV DDLKEVVAAN 400
    KEDRVRKAMD AQAIITDESK HFEAWRDSLE TVPTIKKLRG YTERIIAAEI 450
    EKSLPKMGID MNKKMRKTVD DLIRGIVNKL LHGPMQHLRC DGNDSRTLSE 500
    TLDNMQALNR MYGLDAEILE EKIRAKVEKK 530
    Length:530
    Mass (Da):58,292
    Last modified:July 24, 2007 - v2
    Checksum:i0C0224296BA3D0A8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti245 – 2451A → G in BAF00558. 1 PublicationCurated
    Sequence conflicti410 – 4101D → E in AAB01674. (PubMed:8605295)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U27118 Genomic DNA. Translation: AAB01674.1.
    AC000132 Genomic DNA. Translation: AAB60749.1.
    CP002684 Genomic DNA. Translation: AEE28519.1.
    BT023439 mRNA. Translation: AAY56430.1.
    AK228651 mRNA. Translation: BAF00558.1.
    PIRiG86233.
    S65773.
    RefSeqiNP_172465.1. NM_100868.2.
    UniGeneiAt.27711.

    Genome annotation databases

    EnsemblPlantsiAT1G09940.1; AT1G09940.1; AT1G09940.
    GeneIDi837528.
    KEGGiath:AT1G09940.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U27118 Genomic DNA. Translation: AAB01674.1 .
    AC000132 Genomic DNA. Translation: AAB60749.1 .
    CP002684 Genomic DNA. Translation: AEE28519.1 .
    BT023439 mRNA. Translation: AAY56430.1 .
    AK228651 mRNA. Translation: BAF00558.1 .
    PIRi G86233.
    S65773.
    RefSeqi NP_172465.1. NM_100868.2.
    UniGenei At.27711.

    3D structure databases

    ProteinModelPortali P49294.
    SMRi P49294. Positions 88-415.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P49294.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G09940.1 ; AT1G09940.1 ; AT1G09940 .
    GeneIDi 837528.
    KEGGi ath:AT1G09940.

    Organism-specific databases

    TAIRi AT1G09940.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    InParanoidi P49294.
    KOi K02492.
    OMAi AITCGKK.
    PhylomeDBi P49294.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    UPA00668 .
    BioCyci ARA:AT1G09940-MONOMER.
    MetaCyc:AT1G09940-MONOMER.

    Gene expression databases

    Genevestigatori P49294.

    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. "A second and differentially expressed glutamyl-tRNA reductase gene from Arabidopsis thaliana."
      Kumar A.M., Csankovszki G., Soell D.
      Plant Mol. Biol. 30:419-426(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
      Strain: cv. Columbia.
    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. "Arabidopsis ORF clones."
      Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.
      Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
      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. "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.
    7. "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.
    8. "Induction of isoforms of tetrapyrrole biosynthetic enzymes, AtHEMA2 and AtFC1, under stress conditions and their physiological functions in Arabidopsis."
      Nagai S., Koide M., Takahashi S., Kikuta A., Aono M., Sasaki-Sekimoto Y., Ohta H., Takamiya K., Masuda T.
      Plant Physiol. 144:1039-1051(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION BY WOUNDING AND REACTIVE OXYGEN SPECIES, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiHEM12_ARATH
    AccessioniPrimary (citable) accession number: P49294
    Secondary accession number(s): O04950, Q0WQP1, Q4V3B7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: July 24, 2007
    Last modified: October 1, 2014
    This is version 123 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

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3