Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9KQ24

- HEM1_VIBCH

UniProt

Q9KQ24 - HEM1_VIBCH

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • 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
    Sitei97 – 971Important for activityUniRule annotation
    Binding sitei107 – 1071SubstrateUniRule annotation
    Binding sitei118 – 1181SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi187 – 1926NADPUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. porphyrin-containing compound biosynthetic process Source: TIGR
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciVCHO:VC2180-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:VC_2180
    OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
    Taxonomic identifieri243277 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000000584: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 419419Glutamyl-tRNA reductasePRO_0000114083Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi243277.VC2180.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9KQ24.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni112 – 1143Substrate 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.
    KOiK02492.
    OMAiHEVTGEY.
    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.

    Q9KQ24-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLLAIGINH NTASVELREK VAFGPEKLSL ALNQLSTSSH VKGGVILSTC    50
    NRTEIYCDVR SASKNKVIEW LSQFHQVSLD ELKPSLYVHE EQAAIRHLMR 100
    VACGLDSLVL GEPQILGQVK QAYAEARENH AVNPATEKLF QKAFSVAKRV 150
    RTETEIGGSA VSVAYAACTL AKHIFESLAD ATVLLVGAGE TIELVAKHLA 200
    GHHCKRMIVA NRTRERALSL AQQFGADVIA LNEIPDYLAQ ADIVISSTAS 250
    PLPIIGKGMV ESALKARRHQ PMLLVDIAVP RDIEPQVGKL NDAYLYSVDD 300
    LQSIVDSNIE QRKVEAIQAE AIVSEESATF MSWMRSLQAV DSIRDYRKQA 350
    NEAREELLNK SLQALAAGGD PEKLLIELSN KLTNKLIHTP TRALQTAAEQ 400
    GEPAKLAVIR QSLGLDDLN 419
    Length:419
    Mass (Da):45,744
    Last modified:October 1, 2000 - v1
    Checksum:i6D2D870AD3EEF8EC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF227752 Genomic DNA. Translation: AAK00701.1.
    AE003852 Genomic DNA. Translation: AAF95325.1.
    PIRiC82109.
    RefSeqiNP_231811.1. NC_002505.1.
    WP_000054219.1. NC_002505.1.

    Genome annotation databases

    EnsemblBacteriaiAAF95325; AAF95325; VC_2180.
    GeneIDi2613316.
    KEGGivch:VC2180.
    PATRICi20083373. VBIVibCho83274_2078.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF227752 Genomic DNA. Translation: AAK00701.1 .
    AE003852 Genomic DNA. Translation: AAF95325.1 .
    PIRi C82109.
    RefSeqi NP_231811.1. NC_002505.1.
    WP_000054219.1. NC_002505.1.

    3D structure databases

    ProteinModelPortali Q9KQ24.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243277.VC2180.

    Protocols and materials databases

    DNASUi 2613316.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF95325 ; AAF95325 ; VC_2180 .
    GeneIDi 2613316.
    KEGGi vch:VC2180.
    PATRICi 20083373. VBIVibCho83274_2078.

    Phylogenomic databases

    eggNOGi COG0373.
    KOi K02492.
    OMAi HEVTGEY.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci VCHO:VC2180-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. "Cloning and characterization of hemA and hemM gene of Vibrio cholerae (Bengal strain)."
      Ravichandran M., Lalitha P., Tang T.H., Chan Y.Y., Johari M.R., Zainuddin Z.F.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Bengal.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39315 / El Tor Inaba N16961.

    Entry informationi

    Entry nameiHEM1_VIBCH
    AccessioniPrimary (citable) accession number: Q9KQ24
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 99 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