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Protein

Glutamate synthase [NADPH] large chain

Gene

gltB

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

Protein has several cofactor binding sites:
  • [3Fe-4S] clusterBy similarityNote: Binds 1 [3Fe-4S] cluster.By similarity
  • FAD1 Publication
  • FMN1 Publication

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
    Active sitei12NucleophilePROSITE-ProRule annotation1
    Metal bindingi1102Iron-sulfur (3Fe-4S)By similarity1
    Metal bindingi1108Iron-sulfur (3Fe-4S)By similarity1
    Metal bindingi1113Iron-sulfur (3Fe-4S)By similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi1049 – 1101FMNBy similarityAdd BLAST53

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionOxidoreductase
    Biological processAmino-acid biosynthesis, Glutamate biosynthesis
    Ligand3Fe-4S, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NADP

    Enzyme and pathway databases

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

    Protein family/group databases

    MEROPSiC44.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate synthase [NADPH] large chain (EC:1.4.1.131 Publication)
    Alternative name(s):
    Glutamate synthase subunit alpha
    Short name:
    GLTS alpha chain
    NADPH-GOGAT
    Gene namesi
    Name:gltB
    Synonyms:aspB
    Ordered Locus Names:b3212, JW3179
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10403. gltB.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    PropeptideiPRO_00000116201 – 11Add BLAST11
    ChainiPRO_000001162112 – 1486Glutamate synthase [NADPH] large chainAdd BLAST1475

    Keywords - PTMi

    Zymogen

    Proteomic databases

    PaxDbiP09831.
    PRIDEiP09831.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    gltDP098322EBI-551179,EBI-544293

    Protein-protein interaction databases

    BioGridi4263210. 332 interactors.
    DIPiDIP-9802N.
    IntActiP09831. 8 interactors.
    MINTiMINT-1248755.
    STRINGi316385.ECDH10B_3387.

    Structurei

    3D structure databases

    ProteinModelPortaliP09831.
    SMRiP09831.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini12 – 402Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd BLAST391

    Sequence similaritiesi

    Belongs to the glutamate synthase family.Curated

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiENOG4105CBC. Bacteria.
    COG0067. LUCA.
    COG0069. LUCA.
    COG0070. LUCA.
    HOGENOMiHOG000031558.
    InParanoidiP09831.
    KOiK00265.
    PhylomeDBiP09831.

    Family and domain databases

    CDDicd02808. GltS_FMN. 1 hit.
    Gene3Di2.160.20.60. 1 hit.
    3.20.20.70. 2 hits.
    3.60.20.10. 1 hit.
    InterProiView protein in InterPro
    IPR013785. Aldolase_TIM.
    IPR017932. GATase_2_dom.
    IPR002489. Glu_synth_asu_C.
    IPR006982. Glu_synth_centr_N.
    IPR002932. Glu_synthdom.
    IPR029055. Ntn_hydrolases_N.
    PfamiView protein in Pfam
    PF00310. GATase_2. 1 hit.
    PF04898. Glu_syn_central. 1 hit.
    PF01645. Glu_synthase. 1 hit.
    PF01493. GXGXG. 1 hit.
    SUPFAMiSSF56235. SSF56235. 1 hit.
    SSF69336. SSF69336. 1 hit.
    PROSITEiView protein in PROSITE
    PS51278. GATASE_TYPE_2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P09831-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLYDKSLERD NCGFGLIAHI EGEPSHKVVR TAIHALARMQ HRGAILADGK
    60 70 80 90 100
    TGDGCGLLLQ KPDRFFRIVA QERGWRLAKN YAVGMLFLNK DPELAAAARR
    110 120 130 140 150
    IVEEELQRET LSIVGWRDVP TNEGVLGEIA LSSLPRIEQI FVNAPAGWRP
    160 170 180 190 200
    RDMERRLFIA RRRIEKRLEA DKDFYVCSLS NLVNIYKGLC MPTDLPRFYL
    210 220 230 240 250
    DLADLRLESA ICLFHQRFST NTVPRWPLAQ PFRYLAHNGE INTITGNRQW
    260 270 280 290 300
    ARARTYKFQT PLIPDLHDAA PFVNETGSDS SSMDNMLELL LAGGMDIIRA
    310 320 330 340 350
    MRLLVPPAWQ NNPDMDPELR AFFDFNSMHM EPWDGPAGIV MSDGRFAACN
    360 370 380 390 400
    LDRNGLRPAR YVITKDKLIT CASEVGIWDY QPDEVVEKGR VGPGELMVID
    410 420 430 440 450
    TRSGRILHSA ETDDDLKSRH PYKEWMEKNV RRLVPFEDLP DEEVGSRELD
    460 470 480 490 500
    DDTLASYQKQ FNYSAEELDS VIRVLGENGQ EAVGSMGDDT PFAVLSSQPR
    510 520 530 540 550
    IIYDYFRQQF AQVTNPPIDP LREAHVMSLA TSIGREMNVF CEAEGQAHRL
    560 570 580 590 600
    SFKSPILLYS DFKQLTTMKE EHYRADTLDI TFDVTKTTLE ATVKELCDKA
    610 620 630 640 650
    EKMVRSGTVL LVLSDRNIAK DRLPVPAPMA VGAIQTRLVD QSLRCDANII
    660 670 680 690 700
    VETASARDPH HFAVLLGFGA TAIYPYLAYE TLGRLVDTHA IAKDYRTVML
    710 720 730 740 750
    NYRNGINKGL YKIMSKMGIS TIASYRCSKL FEAVGLHDDV VGLCFQGAVS
    760 770 780 790 800
    RIGGASFEDF QQDLLNLSKR AWLARKPISQ GGLLKYVHGG EYHAYNPDVV
    810 820 830 840 850
    RTLQQAVQSG EYSDYQEYAK LVNERPATTL RDLLAITPGE NAVNIADVEP
    860 870 880 890 900
    ASELFKRFDT AAMSIGALSP EAHEALAEAM NSIGGNSNSG EGGEDPARYG
    910 920 930 940 950
    TNKVSRIKQV ASGRFGVTPA YLVNADVIQI KVAQGAKPGE GGQLPGDKVT
    960 970 980 990 1000
    PYIAKLRYSV PGVTLISPPP HHDIYSIEDL AQLIFDLKQV NPKAMISVKL
    1010 1020 1030 1040 1050
    VSEPGVGTIA TGVAKAYADL ITIAGYDGGT GASPLSSVKY AGCPWELGLV
    1060 1070 1080 1090 1100
    ETQQALVANG LRHKIRLQVD GGLKTGVDII KAAILGAESF GFGTGPMVAL
    1110 1120 1130 1140 1150
    GCKYLRICHL NNCATGVATQ DDKLRKNHYH GLPFKVTNYF EFIARETREL
    1160 1170 1180 1190 1200
    MAQLGVTRLV DLIGRTDLLK ELDGFTAKQQ KLALSKLLET AEPHPGKALY
    1210 1220 1230 1240 1250
    CTENNPPFDN GLLNAQLLQQ AKPFVDERQS KTFWFDIRNT DRSVGASLSG
    1260 1270 1280 1290 1300
    YIAQTHGDQG LAADPIKAYF NGTAGQSFGV WNAGGVELYL TGDANDYVGK
    1310 1320 1330 1340 1350
    GMAGGLIAIR PPVGSAFRSH EASIIGNTCL YGATGGRLYA AGRAGERFGV
    1360 1370 1380 1390 1400
    RNSGAITVVE GIGDNGCEYM TGGIVCILGK TGVNFGAGMT GGFAYVLDES
    1410 1420 1430 1440 1450
    GDFRKRVNPE LVEVLSVDAL AIHEEHLRGL ITEHVQHTGS QRGEEILANW
    1460 1470 1480
    STFATKFALV KPKSSDVKAL LGHRSRSAAE LRVQAQ
    Length:1,486
    Mass (Da):163,297
    Last modified:November 30, 2010 - v3
    Checksum:i19C1E5B04F94A33D
    GO

    Sequence cautioni

    The sequence AAA23904 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence AAA23906 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence AAA58014 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAE77256 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti74 – 78GWRLA → LAFR in AAA23904 (PubMed:3326786).Curated5
    Sequence conflicti109E → N in AAA23904 (PubMed:3326786).Curated1
    Sequence conflicti189 – 209LCMPT…LRLES → CVCRRICRVLSGSCGPASGM in AAA23904 (PubMed:3326786).CuratedAdd BLAST21
    Sequence conflicti228 – 251LAQPF…NRQWA → WRNRSAIWRITVKSTPSPVT ANG in AAA23904 (PubMed:3326786).CuratedAdd BLAST24
    Sequence conflicti228 – 251LAQPF…NRQWA → WRNRSAIWRITVKSTPSPVT ANG in AAA23906 (PubMed:1673677).CuratedAdd BLAST24
    Sequence conflicti429N → K in AAA23904 (PubMed:3326786).Curated1
    Sequence conflicti543A → T in AAA23904 (PubMed:3326786).Curated1
    Sequence conflicti832D → H in AAA23904 (PubMed:3326786).Curated1
    Sequence conflicti1255 – 1259THGDQ → DARRS in AAA23904 (PubMed:3326786).Curated5
    Sequence conflicti1342G → A in AAA23904 (PubMed:3326786).Curated1
    Sequence conflicti1345G → R in AAA23904 (PubMed:3326786).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M18747 Genomic DNA. Translation: AAA23904.1. Different initiation.
    U18997 Genomic DNA. Translation: AAA58014.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76244.2.
    AP009048 Genomic DNA. Translation: BAE77256.1. Different initiation.
    M68876 Genomic DNA. Translation: AAA23906.1. Different initiation.
    PIRiF65112.
    RefSeqiNP_417679.2. NC_000913.3.
    WP_001300352.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76244; AAC76244; b3212.
    BAE77256; BAE77256; BAE77256.
    GeneIDi947724.
    KEGGiecj:JW3179.
    eco:b3212.
    PATRICifig|511145.12.peg.3307.

    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 nameiGLTB_ECOLI
    AccessioniPrimary (citable) accession number: P09831
    Secondary accession number(s): Q2M900
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 30, 2010
    Last modified: July 5, 2017
    This is version 157 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
    3. SIMILARITY comments
      Index of protein domains and families