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A7HBF2

- HEM12_ANADF

UniProt

A7HBF2 - HEM12_ANADF

Protein

Glutamyl-tRNA reductase 2

Gene

hemA2

Organism
Anaeromyxobacter sp. (strain Fw109-5)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 2 (20 May 2008)
      Previous versions | rss
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    • 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 sitei49 – 491NucleophileUniRule annotation
    Sitei93 – 931Important for activityUniRule annotation
    Binding sitei103 – 1031SubstrateUniRule annotation
    Binding sitei114 – 1141SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi183 – 1886NADPUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciASP404589:GHMT-1856-MONOMER.
    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductase 2UniRule annotation (EC:1.2.1.70UniRule annotation)
    Short name:
    GluTR 2UniRule annotation
    Gene namesi
    Name:hemA2UniRule annotation
    Ordered Locus Names:Anae109_1845
    OrganismiAnaeromyxobacter sp. (strain Fw109-5)
    Taxonomic identifieri404589 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeAnaeromyxobacteraceaeAnaeromyxobacter
    ProteomesiUP000006382: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 423423Glutamyl-tRNA reductase 2PRO_0000335008Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi404589.Anae109_1845.

    Structurei

    3D structure databases

    ProteinModelPortaliA7HBF2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni48 – 514Substrate bindingUniRule annotation
    Regioni108 – 1103Substrate 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.
    HOGENOMiHOG000109651.
    KOiK02492.
    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.
    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.

    A7HBF2-1 [UniParc]FASTAAdd to Basket

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    MLVAVGLNQK GATVADREVL ALPAEGFQST LAEYAALDAV DEIAVMSTCY    50
    RVEIYAATRC PAAATLSLRQ ALNARAGREL PLFELHGEEA YRHLVRVASS 100
    LESAILGEPQ ILGQVKEAFQ RSIDQGVAAK ELTSVLNRAL SAAKRVRTDT 150
    AIGRAGISWG HAAATLAEKV LGKMQGRRVV VVGAGEMARL SAQHLRDQGA 200
    RIVVLNRTLV NGEALAREVG GVARPLEALG EELAQADVVV SAAPVAPDAF 250
    QPEAMAELSR SRKRPIVLVD LAVPRAIPAA TGAIRDVYLC DVDDLDRVMK 300
    AAMSERAAAV ADADRIIAEE VGKFVRAEAE RRAAPLIQEM RTRASAIARE 350
    EVERTLRRLG EDPEVERRLE AMAGSIVSKI LHAPSARLRQ AVCDGCSGEA 400
    LVSAAVEIFE LSADIRVHRG NAA 423
    Length:423
    Mass (Da):45,130
    Last modified:May 20, 2008 - v2
    Checksum:i494272D1FBFC0093
    GO

    Sequence cautioni

    The sequence ABS26048.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000769 Genomic DNA. Translation: ABS26048.1. Different initiation.
    RefSeqiWP_012096626.1. NC_009675.1.
    YP_001379032.1. NC_009675.1.

    Genome annotation databases

    EnsemblBacteriaiABS26048; ABS26048; Anae109_1845.
    GeneIDi5377847.
    KEGGiafw:Anae109_1845.
    PATRICi20928931. VBIAnaSp113478_1943.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000769 Genomic DNA. Translation: ABS26048.1 . Different initiation.
    RefSeqi WP_012096626.1. NC_009675.1.
    YP_001379032.1. NC_009675.1.

    3D structure databases

    ProteinModelPortali A7HBF2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 404589.Anae109_1845.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABS26048 ; ABS26048 ; Anae109_1845 .
    GeneIDi 5377847.
    KEGGi afw:Anae109_1845.
    PATRICi 20928931. VBIAnaSp113478_1943.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci ASP404589:GHMT-1856-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.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Fw109-5.

    Entry informationi

    Entry nameiHEM12_ANADF
    AccessioniPrimary (citable) accession number: A7HBF2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 59 of the entry and version 2 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, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3