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Protein

Glutamate synthase [NADPH] small chain

Gene

gltD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate.1 Publication

Miscellaneous

Glutamine binds to the large subunit and transfers the amido group to 2-oxoglutarate that apparently binds to the small subunit.

Catalytic activityi

2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH.1 Publication

Cofactori

[4Fe-4S] clusterPROSITE-ProRule annotationNote: Binds 1 [4Fe-4S] cluster.PROSITE-ProRule annotation

Kineticsi

  1. KM=7.3 µM for 2-oxoglutarate1 Publication
  2. KM=250 µM for L-glutamine1 Publication

    pH dependencei

    Optimum pH is 7.6.1 Publication

    Pathwayi: L-glutamate biosynthesis via GLT pathway

    This protein is involved in step 1 of the subpathway that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+) route).
    Proteins known to be involved in this subpathway in this organism are:
    1. Glutamate synthase [NADPH] small chain (gltD), Glutamate synthase [NADPH] large chain (gltB)
    This subpathway is part of the pathway L-glutamate biosynthesis via GLT pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+) route), the pathway L-glutamate biosynthesis via GLT pathway and in Amino-acid biosynthesis.

    Pathwayi: nitrogen metabolism

    This protein is involved in the pathway nitrogen metabolism, which is part of Energy metabolism.
    View all proteins of this organism that are known to be involved in the pathway nitrogen metabolism and in Energy metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi47Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation1
    Metal bindingi50Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation1
    Metal bindingi55Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation1
    Metal bindingi59Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation1

    GO - Molecular functioni

    GO - Biological processi

    • glutamate biosynthetic process Source: EcoCyc
    • L-glutamate biosynthetic process Source: UniProtKB-UniPathway

    Keywordsi

    Molecular functionOxidoreductase
    Biological processAmino-acid biosynthesis, Glutamate biosynthesis
    Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:GLUSYNSMALL-MONOMER.
    MetaCyc:GLUSYNSMALL-MONOMER.
    BRENDAi1.4.1.13. 2026.
    UniPathwayiUPA00045.
    UPA00634; UER00689.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate synthase [NADPH] small chain (EC:1.4.1.131 Publication)
    Alternative name(s):
    Glutamate synthase subunit beta
    Short name:
    GLTS beta chain
    NADPH-GOGAT
    Gene namesi
    Name:gltD
    Synonyms:aspB
    Ordered Locus Names:b3213, JW3180
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10404. gltD.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved2 Publications
    ChainiPRO_00001708002 – 472Glutamate synthase [NADPH] small chainAdd BLAST471

    Proteomic databases

    PaxDbiP09832.
    PRIDEiP09832.

    2D gel databases

    SWISS-2DPAGEiP09832.

    Interactioni

    Subunit structurei

    Aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    gltBP098312EBI-544293,EBI-551179

    Protein-protein interaction databases

    BioGridi4262427. 185 interactors.
    DIPiDIP-9803N.
    IntActiP09832. 6 interactors.
    MINTiMINT-1248739.
    STRINGi316385.ECDH10B_3388.

    Structurei

    3D structure databases

    ProteinModelPortaliP09832.
    SMRiP09832.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini38 – 694Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd BLAST32

    Phylogenomic databases

    eggNOGiENOG4105BZ8. Bacteria.
    COG0493. LUCA.
    HOGENOMiHOG000031439.
    InParanoidiP09832.
    KOiK00266.
    PhylomeDBiP09832.

    Family and domain databases

    Gene3Di3.50.50.60. 3 hits.
    InterProiView protein in InterPro
    IPR017896. 4Fe4S_Fe-S-bd.
    IPR028261. DPD_II.
    IPR023753. FAD/NAD-binding_dom.
    IPR006006. Glut_synth_ssu2.
    IPR009051. Helical_ferredxn.
    PfamiView protein in Pfam
    PF14691. Fer4_20. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    SUPFAMiSSF46548. SSF46548. 1 hit.
    TIGRFAMsiTIGR01318. gltD_gamma_fam. 1 hit.
    PROSITEiView protein in PROSITE
    PS51379. 4FE4S_FER_2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P09832-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSQNVYQFID LQRVDPPKKP LKIRKIEFVE IYEPFSEGQA KAQADRCLSC
    60 70 80 90 100
    GNPYCEWKCP VHNYIPNWLK LANEGRIFEA AELSHQTNTL PEVCGRVCPQ
    110 120 130 140 150
    DRLCEGSCTL NDEFGAVTIG NIERYINDKA FEMGWRPDMS GVKQTGKKVA
    160 170 180 190 200
    IIGAGPAGLA CADVLTRNGV KAVVFDRHPE IGGLLTFGIP AFKLEKEVMT
    210 220 230 240 250
    RRREIFTGMG IEFKLNTEVG RDVQLDDLLS DYDAVFLGVG TYQSMRGGLE
    260 270 280 290 300
    NEDADGVYAA LPFLIANTKQ LMGFGETRDE PFVSMEGKRV VVLGGGDTAM
    310 320 330 340 350
    DCVRTSVRQG AKHVTCAYRR DEENMPGSRR EVKNAREEGV EFKFNVQPLG
    360 370 380 390 400
    IEVNGNGKVS GVKMVRTEMG EPDAKGRRRA EIVAGSEHIV PADAVIMAFG
    410 420 430 440 450
    FRPHNMEWLA KHSVELDSQG RIIAPEGSDN AFQTSNPKIF AGGDIVRGSD
    460 470
    LVVTAIAEGR KAADGIMNWL EV
    Length:472
    Mass (Da):52,015
    Last modified:January 23, 2007 - v3
    Checksum:iF188CE1086040433
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti38 – 51GQAKA…CLSCG → ARPKRRLTAACRAA (PubMed:3326786).CuratedAdd BLAST14
    Sequence conflicti123E → K in AAA23905 (PubMed:3326786).Curated1
    Sequence conflicti174V → C in AAA23905 (PubMed:3326786).Curated1
    Sequence conflicti257 – 270VYAAL…ANTKQ → CTQRCRSSSPTPNS (PubMed:3326786).CuratedAdd BLAST14
    Sequence conflicti312 – 313KH → ND in AAA23905 (PubMed:3326786).Curated2
    Sequence conflicti376 – 400GRRRA…IMAFG → ASPRGDRCRFRTYRTGRCGD HGVW in AAA23905 (PubMed:3326786).CuratedAdd BLAST25

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M18747 Genomic DNA. Translation: AAA23905.1.
    U18997 Genomic DNA. Translation: AAA58015.1.
    U00096 Genomic DNA. Translation: AAC76245.1.
    AP009048 Genomic DNA. Translation: BAE77257.1.
    PIRiG65112.
    RefSeqiNP_417680.1. NC_000913.3.
    WP_000081674.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76245; AAC76245; b3213.
    BAE77257; BAE77257; BAE77257.
    GeneIDi947723.
    KEGGiecj:JW3180.
    eco:b3213.
    PATRICifig|511145.12.peg.3308.

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

    Entry informationi

    Entry nameiGLTD_ECOLI
    AccessioniPrimary (citable) accession number: P09832
    Secondary accession number(s): Q2M8Z9
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: July 5, 2017
    This is version 167 of the entry and version 3 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways