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Q9UXR8

- HEM1_METKA

UniProt

Q9UXR8 - HEM1_METKA

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA.1 Publication

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by heavy metal compounds, Zn2+, and heme. Also competitively inhibited by glutamycin.

    pH dependencei

    Optimum pH is 8.1.

    Temperature dependencei

    Optimum temperature is 90 degrees Celsius.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei48 – 481Nucleophile
    Sitei84 – 841Important for activity
    Binding sitei94 – 941Substrate
    Binding sitei105 – 1051Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi174 – 1796NADPCurated

    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

    BRENDAi1.2.1.70. 3274.
    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductase (EC:1.2.1.70)
    Short name:
    GluTR
    Gene namesi
    Name:hemA
    Ordered Locus Names:MK0200
    OrganismiMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
    Taxonomic identifieri190192 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus
    ProteomesiUP000001826: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi48 – 481C → S: Complete loss of activity. 1 Publication
    Mutagenesisi84 – 841H → A: Complete loss of activity. 1 Publication
    Mutagenesisi84 – 841H → N: 30% of wild-type reductase activity. 15% of wild-type esterase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 404404Glutamyl-tRNA reductasePRO_0000114102Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi190192.MK0200.

    Structurei

    Secondary structure

    1
    404
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107
    Turni11 – 133
    Helixi16 – 227
    Helixi29 – 368
    Beta strandi40 – 478
    Beta strandi50 – 578
    Helixi62 – 676
    Beta strandi74 – 774
    Helixi78 – 8912
    Turni90 – 934
    Beta strandi94 – 963
    Helixi100 – 11617
    Helixi121 – 14020
    Helixi150 – 16213
    Beta strandi169 – 1746
    Helixi177 – 18913
    Beta strandi192 – 1976
    Helixi201 – 21111
    Helixi218 – 2203
    Helixi221 – 2266
    Beta strandi229 – 2335
    Beta strandi236 – 2394
    Helixi244 – 25310
    Beta strandi260 – 2645
    Helixi275 – 2773
    Beta strandi281 – 2855
    Helixi286 – 30116
    Helixi304 – 35047
    Helixi365 – 38218
    Turni386 – 3905
    Helixi391 – 40212

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GPJX-ray1.95A1-404[»]
    ProteinModelPortaliQ9UXR8.
    SMRiQ9UXR8. Positions 1-404.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UXR8.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni47 – 504Substrate binding
    Regioni99 – 1013Substrate binding

    Sequence similaritiesi

    Belongs to the glutamyl-tRNA reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0373.
    HOGENOMiHOG000109651.
    KOiK02492.
    OMAiYREADAN.

    Family and domain databases

    Gene3Di1.10.1200.70. 1 hit.
    3.40.50.720. 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.

    Q9UXR8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEDLVCVGIT HKEAEVEELE KARFESDEAV RDIVESFGLS GCVLLQTCNR    50
    VEVYASGARD RAEELGDLIH DDAWVKRGSE AVRHLFRVAC GLESMMVGEQ 100
    EILRQVKKAY DRAARLGTLD EALKIVFRRA INLGKRAREE TRISEGAVSI 150
    GSAAVELAER ELGSLHDKTV LVVGAGEMGK TVAKSLVDRG VRAVLVANRT 200
    YERAVELARD LGGEAVRFDE LVDHLARSDV VVSATAAPHP VIHVDDVREA 250
    LRKRDRRSPI LIIDIANPRD VEEGVENIED VEVRTIDDLR VIARENLERR 300
    RKEIPKVEKL IEEELSTVEE ELEKLKERRL VADVAKSLHE IKDRELERAL 350
    RRLKTGDPEN VLQDFAEAYT KRLINVLTSA IMELPDEYRR AACRALRRAS 400
    ELNG 404
    Length:404
    Mass (Da):45,444
    Last modified:May 1, 2000 - v1
    Checksum:i8B6DBE436EA073B3
    GO

    Mass spectrometryi

    Molecular mass is 45436±30 Da from positions 1 - 404. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ131561 Genomic DNA. Translation: CAB59204.1.
    AE009439 Genomic DNA. Translation: AAM01417.1.
    PIRiT45026.
    RefSeqiNP_613487.1. NC_003551.1.
    WP_011018572.1. NC_003551.1.

    Genome annotation databases

    EnsemblBacteriaiAAM01417; AAM01417; MK0200.
    GeneIDi1477503.
    KEGGimka:MK0200.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ131561 Genomic DNA. Translation: CAB59204.1 .
    AE009439 Genomic DNA. Translation: AAM01417.1 .
    PIRi T45026.
    RefSeqi NP_613487.1. NC_003551.1.
    WP_011018572.1. NC_003551.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GPJ X-ray 1.95 A 1-404 [» ]
    ProteinModelPortali Q9UXR8.
    SMRi Q9UXR8. Positions 1-404.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 190192.MK0200.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM01417 ; AAM01417 ; MK0200 .
    GeneIDi 1477503.
    KEGGi mka:MK0200.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OMAi YREADAN.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BRENDAi 1.2.1.70. 3274.

    Miscellaneous databases

    EvolutionaryTracei Q9UXR8.

    Family and domain databases

    Gene3Di 1.10.1200.70. 1 hit.
    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 [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30, FUNCTION, MASS SPECTROMETRY, CATALYTIC MECHANISM, MUTAGENESIS OF CYS-48 AND HIS-84.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.
    3. "V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis."
      Moser J., Schubert W.-D., Beier V., Bringemeier I., Jahn D., Heinz D.W.
      EMBO J. 20:6583-6590(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT, CATALYTIC MECHANISM, DOMAIN.

    Entry informationi

    Entry nameiHEM1_METKA
    AccessioniPrimary (citable) accession number: Q9UXR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 116 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3