Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

B8G817

- HEM1_CHLAD

UniProt

B8G817 - HEM1_CHLAD

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chloroflexus aggregans (strain MD-66 / DSM 9485)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (03 Mar 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei55 – 551NucleophileUniRule annotation
    Sitei103 – 1031Important for activityUniRule annotation
    Binding sitei113 – 1131SubstrateUniRule annotation
    Binding sitei124 – 1241SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi193 – 1986NADPUniRule annotation

    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

    BioCyciCAGG326427:GHS8-1301-MONOMER.
    UniPathwayiUPA00251; UER00316.
    UPA00668.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
    Short name:
    GluTRUniRule annotation
    Gene namesi
    Name:hemAUniRule annotation
    Ordered Locus Names:Cagg_1288
    OrganismiChloroflexus aggregans (strain MD-66 / DSM 9485)
    Taxonomic identifieri326427 [NCBI]
    Taxonomic lineageiBacteriaChloroflexiChloroflexiaChloroflexalesChloroflexineaeChloroflexaceaeChloroflexus
    ProteomesiUP000002508: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 453453Glutamyl-tRNA reductasePRO_1000190511Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi326427.Cagg_1288.

    Structurei

    3D structure databases

    ProteinModelPortaliB8G817.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni54 – 574Substrate bindingUniRule annotation
    Regioni118 – 1203Substrate bindingUniRule annotation

    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.UniRule annotation

    Sequence similaritiesi

    Belongs to the glutamyl-tRNA reductase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0373.
    HOGENOMiHOG000109650.
    KOiK02492.
    OMAiLAHKLTN.
    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.
    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.

    Sequencei

    Sequence statusi: Complete.

    B8G817-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNLFLAGLDH TTAPVEIREQ LAFSQTDLPS ALLQLTQADN GSPPLFTEAV    50
    ILSTCNRVEI YGVANPGTTA QHVVDFLANF HRRPAGSFVH TLYFYQGEAV 100
    ARHLCATAAG LRSLVLGEAQ IQGQVRSAYE AAQRIGSVGS VLHRLFQIAL 150
    VAGKRVRHET TIGKGAASVS QAGVELARRR LGDLRGREVL LIGGGEVSEL 200
    AAQNLIANGA DRLTIVNRTS SRAAALAERY GAEMLDFGAL PEALARADIV 250
    ISSTAAPVPI IYRHHIAEAL SHKQRMRACG DCDPPAMLLI DLAVPRDIAA 300
    DVAELPGVYL FTVDDLREVV SHTIELRSAV IDIANQIVEE QVREFSDWLR 350
    TQEALPVLTM LRQRAEEVRN EELTRALRRL HDLSPEQRAV IEGLSRSIVN 400
    KLLHPPTRCL REAAAHGQGK RYATMLAELF NLEHALEHKA GAMGNTELTD 450
    RMR 453
    Length:453
    Mass (Da):49,496
    Last modified:March 3, 2009 - v1
    Checksum:i4D3B325E808BA6CE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001337 Genomic DNA. Translation: ACL24196.1.
    RefSeqiWP_012616560.1. NC_011831.1.
    YP_002462632.1. NC_011831.1.

    Genome annotation databases

    EnsemblBacteriaiACL24196; ACL24196; Cagg_1288.
    GeneIDi7266274.
    KEGGicag:Cagg_1288.
    PATRICi21405082. VBIChlAgg85409_1336.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001337 Genomic DNA. Translation: ACL24196.1 .
    RefSeqi WP_012616560.1. NC_011831.1.
    YP_002462632.1. NC_011831.1.

    3D structure databases

    ProteinModelPortali B8G817.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 326427.Cagg_1288.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACL24196 ; ACL24196 ; Cagg_1288 .
    GeneIDi 7266274.
    KEGGi cag:Cagg_1288.
    PATRICi 21405082. VBIChlAgg85409_1336.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    UPA00668 .
    BioCyci CAGG326427:GHS8-1301-MONOMER.

    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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence of Chloroflexus aggregans DSM 9485."
      US DOE Joint Genome Institute
      Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.
      Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MD-66 / DSM 9485.

    Entry informationi

    Entry nameiHEM1_CHLAD
    AccessioniPrimary (citable) accession number: B8G817
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: March 3, 2009
    Last modified: October 1, 2014
    This is version 43 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.UniRule annotation

    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