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A7ZD34

- HEM1_CAMC1

UniProt

A7ZD34 - HEM1_CAMC1

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Campylobacter concisus (strain 13826)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (23 Oct 2007)
      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 sitei51 – 511NucleophileUniRule annotation
    Sitei100 – 1001Important for activityUniRule annotation
    Binding sitei110 – 1101SubstrateUniRule annotation
    Binding sitei121 – 1211SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi190 – 1956NADPUniRule 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

    BioCyciCCON360104:GHAC-869-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:Ccon26_08200
    ORF Names:CCC13826_1051
    OrganismiCampylobacter concisus (strain 13826)
    Taxonomic identifieri360104 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
    ProteomesiUP000001121: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 427427Glutamyl-tRNA reductasePRO_1000071246Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi360104.CCC13826_1051.

    Structurei

    3D structure databases

    ProteinModelPortaliA7ZD34.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 534Substrate bindingUniRule annotation
    Regioni115 – 1173Substrate 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.

    A7ZD34-1 [UniParc]FASTAAdd to Basket

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    MHYLDISFTY KNTDISVREK LAFDSDEKKE QILKLINSNK NIKESMVLNT    50
    CNRVEIIASV EDVKAATAHI IRCMSIFSGV FEDELYERAD IYENSGAAHH 100
    LFAVASSLDS LVVGETQIVG QLKNAFKFAY DNNSCGEDIS KIIHYACKCA 150
    AKVRNETQIS KNPISVSSVA VAKAKEIFGT LEGKTAIVVG AGEMGELAAK 200
    HLISSGAEVI IINRSSERVE QLVDSLGDNA SWDSILKLKE YVNNYDLIFS 250
    STAAPHAIIT GEIIEPREFH RYFFDIAVPR DIDLLNTELI SVYTVDSLEE 300
    IVRKNLALRE EQAQKAYSIV GQDTSEFLKT LKEDMSVPLI KSIRKQAEIC 350
    AKNELEKAIK KGYLKHSDYD EAQKLIHQVF KAFLHQPTMK LKGLADEERA 400
    SELSNGVKFL FDIKDEQNFQ AGDIDEI 427
    Length:427
    Mass (Da):47,802
    Last modified:October 23, 2007 - v1
    Checksum:i618EE0892BDB953A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000792 Genomic DNA. Translation: EAT97817.1.
    RefSeqiWP_012001638.1. NC_009802.1.
    YP_001466692.1. NC_009802.1.

    Genome annotation databases

    EnsemblBacteriaiEAT97817; EAT97817; CCC13826_1051.
    GeneIDi5595979.
    KEGGicco:CCC13826_1051.
    PATRICi20027839. VBICamCon95352_0862.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000792 Genomic DNA. Translation: EAT97817.1 .
    RefSeqi WP_012001638.1. NC_009802.1.
    YP_001466692.1. NC_009802.1.

    3D structure databases

    ProteinModelPortali A7ZD34.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 360104.CCC13826_1051.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai EAT97817 ; EAT97817 ; CCC13826_1051 .
    GeneIDi 5595979.
    KEGGi cco:CCC13826_1051.
    PATRICi 20027839. VBICamCon95352_0862.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CCON360104:GHAC-869-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. "Genome sequence of Campylobacter concisus 13826 isolated from human feces."
      Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., On S., Nelson K.E.
      Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 13826.

    Entry informationi

    Entry nameiHEM1_CAMC1
    AccessioniPrimary (citable) accession number: A7ZD34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: October 23, 2007
    Last modified: October 1, 2014
    This is version 56 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