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B1I4J1

- HEM1_DESAP

UniProt

B1I4J1 - HEM1_DESAP

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Desulforudis audaxviator (strain MP104C)
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 (29 Apr 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 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

    BioCyciDAUD477974:GH0B-1377-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:Daud_1348
    OrganismiDesulforudis audaxviator (strain MP104C)
    Taxonomic identifieri477974 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeCandidatus Desulforudis
    ProteomesiUP000008544: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 446446Glutamyl-tRNA reductasePRO_1000093131Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi477974.Daud_1348.

    Structurei

    3D structure databases

    ProteinModelPortaliB1I4J1.
    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.
    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.

    B1I4J1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLITVVGLNH RTAPLAVREK LSFPEHTLKE VLRGLSDREG VESCVVISTC    50
    NRTEVYAVLS EEDGLQNIWC FLAERCGSPV EAIKSHTYNY SFGESVRHLF 100
    RVSSGLDSMV LGETQILGQV KQAYQFAQQV GTVNWLLNCA FQQALAVGKR 150
    VRTETGIDKN PVSISYAAVE LARQTLGSLE GREVLIVGAG KMSELTVKHL 200
    LSHGVAGVIV SNRSYPRAVE LAAQFGGRAV RFDELYRWMG HADIVISCTA 250
    ASHYVIRAEP MTSVLAERGG RAIFFIDIAV PRDVDPAVGH LPGVVLYDID 300
    SLQSVVDANL AERRRAAVAA ERIIDAEVRE FLLALGSRFV IPTVVALKKR 350
    GEEIKRNELD RALNRLGGEL SERELKVISS MANSIVSQLL HEPITRLKKL 400
    ALTPEGHFYS DALQKLFNLE PENGGVPTLV GRTESCPVSC LKGKGC 446
    Length:446
    Mass (Da):48,858
    Last modified:April 29, 2008 - v1
    Checksum:i63B174393A2941FB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000860 Genomic DNA. Translation: ACA59857.1.
    RefSeqiWP_012302442.1. NC_010424.1.
    YP_001717489.1. NC_010424.1.

    Genome annotation databases

    EnsemblBacteriaiACA59857; ACA59857; Daud_1348.
    GeneIDi6026143.
    KEGGidau:Daud_1348.
    PATRICi31969510. VBICanDes92303_1392.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000860 Genomic DNA. Translation: ACA59857.1 .
    RefSeqi WP_012302442.1. NC_010424.1.
    YP_001717489.1. NC_010424.1.

    3D structure databases

    ProteinModelPortali B1I4J1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 477974.Daud_1348.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACA59857 ; ACA59857 ; Daud_1348 .
    GeneIDi 6026143.
    KEGGi dau:Daud_1348.
    PATRICi 31969510. VBICanDes92303_1392.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci DAUD477974:GH0B-1377-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. "Complete sequence of chromosome of Desulforudis audaxviator MP104C."
      Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L., Hauser L., Kyrpides N., Ivanova N.N., Richardson P.
      Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MP104C.

    Entry informationi

    Entry nameiHEM1_DESAP
    AccessioniPrimary (citable) accession number: B1I4J1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: April 29, 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