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B2ULP2

- HEM1_AKKM8

UniProt

B2ULP2 - HEM1_AKKM8

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Akkermansia muciniphila (strain ATCC BAA-835)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (01 Jul 2008)
      Previous versions | rss
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    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 sitei50 – 501NucleophileUniRule annotation
    Sitei98 – 981Important for activityUniRule annotation
    Binding sitei108 – 1081SubstrateUniRule annotation
    Binding sitei119 – 1191SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi188 – 1936NADPUniRule 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

    BioCyciAMUC349741:GHZ7-99-MONOMER.
    UniPathwayiUPA00251; UER00316.

    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:Amuc_0091
    OrganismiAkkermansia muciniphila (strain ATCC BAA-835)
    Taxonomic identifieri349741 [NCBI]
    Taxonomic lineageiBacteriaVerrucomicrobiaVerrucomicrobiaeVerrucomicrobialesVerrucomicrobiaceaeAkkermansia
    ProteomesiUP000001031: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 340340Glutamyl-tRNA reductasePRO_1000093112Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi349741.Amuc_0091.

    Structurei

    3D structure databases

    ProteinModelPortaliB2ULP2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni113 – 1153Substrate 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.
    OMAiLNKQFET.
    OrthoDBiEOG6MWNBM.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00087. Glu_tRNA_reductase.
    InterProiIPR000343. 4pyrrol_synth_GluRdtase.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view]
    PfamiPF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
    SUPFAMiSSF69742. SSF69742. 1 hit.
    TIGRFAMsiTIGR01035. hemA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    B2ULP2-1 [UniParc]FASTAAdd to Basket

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    MRMVCLGLNH RTAPVEIRER FAVPSHKLRE EGQRIRSLPG VDQCVVLSTC    50
    NRMEIYYWSN APENAQEHIL SHFLGDGRGE LDMASYFYSH QGEDALGHLC 100
    RVLSGLDSMV LGETEIFGQV KTAYQTALDA GVTAACANKT FQKAFTIGKK 150
    VRTESQIHAG ATSVGSVAVE LAEQIFGDLS GTRVLILGAG EMSRVTGRAL 200
    HARGAEGIYV ANRSFDRAVE LAGMIGGQAI RYDVWGNYLR DIDVVVAATA 250
    APHCIITRET LLPLRASRKY RSLFLIDISV PRNISPDVAD IDEVYLYDID 300
    TLTQLADEAK RSRKQEVSRC EAIIRDSISR YFPDSALYDQ 340
    Length:340
    Mass (Da):37,606
    Last modified:July 1, 2008 - v1
    Checksum:i27D3C2F5FF5D3612
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001071 Genomic DNA. Translation: ACD03936.1.
    RefSeqiWP_012419151.1. NC_010655.1.
    YP_001876717.1. NC_010655.1.

    Genome annotation databases

    EnsemblBacteriaiACD03936; ACD03936; Amuc_0091.
    GeneIDi6274993.
    KEGGiamu:Amuc_0091.
    PATRICi20832684. VBIAkkMuc16855_0109.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001071 Genomic DNA. Translation: ACD03936.1 .
    RefSeqi WP_012419151.1. NC_010655.1.
    YP_001876717.1. NC_010655.1.

    3D structure databases

    ProteinModelPortali B2ULP2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 349741.Amuc_0091.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACD03936 ; ACD03936 ; Amuc_0091 .
    GeneIDi 6274993.
    KEGGi amu:Amuc_0091.
    PATRICi 20832684. VBIAkkMuc16855_0109.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci AMUC349741:GHZ7-99-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_00087. Glu_tRNA_reductase.
    InterProi IPR000343. 4pyrrol_synth_GluRdtase.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view ]
    Pfami PF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
    SUPFAMi SSF69742. SSF69742. 1 hit.
    TIGRFAMsi TIGR01035. hemA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The genome of Akkermansia muciniphila, a dedicated intestinal mucin degrader, and its use in exploring intestinal metagenomes."
      van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M., Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.
      PLoS ONE 6:E16876-E16876(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-835.

    Entry informationi

    Entry nameiHEM1_AKKM8
    AccessioniPrimary (citable) accession number: B2ULP2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 51 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, 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