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P17169

- GLMS_ECOLI

UniProt

P17169 - GLMS_ECOLI

Protein

Glutamine--fructose-6-phosphate aminotransferase [isomerizing]

Gene

glmS

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.

    Catalytic activityi

    L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei2 – 21Nucleophile; for GATase activityBy similarity
    Active sitei604 – 6041For Fru-6P isomerization activity

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. glutamine-fructose-6-phosphate transaminase (isomerizing) activity Source: EcoCyc
    3. protein binding Source: IntAct

    GO - Biological processi

    1. carbohydrate biosynthetic process Source: InterPro
    2. glutamine metabolic process Source: UniProtKB-HAMAP
    3. UDP-N-acetylglucosamine biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Enzyme and pathway databases

    BioCyciEcoCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER.
    ECOL316407:JW3707-MONOMER.
    MetaCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (EC:2.6.1.16)
    Alternative name(s):
    D-fructose-6-phosphate amidotransferase
    GFAT
    Glucosamine-6-phosphate synthase
    Hexosephosphate aminotransferase
    L-glutamine--D-fructose-6-phosphate amidotransferase
    Gene namesi
    Name:glmS
    Ordered Locus Names:b3729, JW3707
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10382. glmS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 609608Glutamine--fructose-6-phosphate aminotransferase [isomerizing]PRO_0000135328Add
    BLAST

    Proteomic databases

    PaxDbiP17169.
    PRIDEiP17169.

    Expressioni

    Gene expression databases

    GenevestigatoriP17169.

    Interactioni

    Subunit structurei

    Homodimer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ynbDP760933EBI-551022,EBI-551038

    Protein-protein interaction databases

    DIPiDIP-9775N.
    IntActiP17169. 8 interactions.
    MINTiMINT-1238536.
    STRINGi511145.b3729.

    Structurei

    Secondary structure

    1
    609
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Helixi14 – 2411
    Helixi25 – 273
    Beta strandi30 – 378
    Beta strandi43 – 508
    Helixi52 – 6110
    Beta strandi67 – 748
    Beta strandi77 – 793
    Turni83 – 853
    Beta strandi89 – 913
    Beta strandi94 – 1029
    Helixi105 – 11410
    Helixi125 – 13713
    Helixi142 – 1498
    Helixi150 – 1523
    Beta strandi155 – 1639
    Beta strandi170 – 1778
    Beta strandi180 – 1834
    Beta strandi188 – 1936
    Helixi194 – 1963
    Turni197 – 2004
    Beta strandi202 – 2065
    Beta strandi212 – 2154
    Beta strandi220 – 2234
    Beta strandi225 – 2273
    Beta strandi234 – 2363
    Turni241 – 2444
    Helixi252 – 2587
    Helixi260 – 2689
    Beta strandi271 – 2733
    Beta strandi274 – 2774
    Helixi280 – 2823
    Helixi286 – 2927
    Beta strandi295 – 3006
    Helixi302 – 31817
    Beta strandi323 – 3275
    Helixi328 – 3325
    Beta strandi342 – 35110
    Helixi354 – 36310
    Turni364 – 3674
    Beta strandi369 – 3779
    Helixi381 – 3855
    Beta strandi386 – 3916
    Beta strandi399 – 4013
    Helixi404 – 42320
    Helixi428 – 44821
    Helixi449 – 4513
    Helixi454 – 4629
    Beta strandi466 – 4727
    Helixi474 – 4763
    Helixi477 – 49115
    Beta strandi494 – 4996
    Helixi500 – 5056
    Helixi507 – 5104
    Beta strandi517 – 5215
    Helixi524 – 53613
    Helixi537 – 5404
    Beta strandi544 – 5496
    Helixi550 – 5523
    Beta strandi560 – 5656
    Helixi570 – 5723
    Helixi573 – 59220
    Beta strandi596 – 5983

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JXAX-ray3.10A/B/C2-609[»]
    1MOQX-ray1.57A242-609[»]
    1MORX-ray1.90A242-609[»]
    1MOSX-ray2.00A242-609[»]
    1XFFX-ray1.80A/B2-241[»]
    1XFGX-ray1.85A/B2-241[»]
    2J6HX-ray2.35A/B2-609[»]
    2VF4X-ray2.95X2-609[»]
    2VF5X-ray2.90X2-609[»]
    3OOJX-ray2.50A/B/C/D/E/F/G/H3-609[»]
    4AMVX-ray2.05A/B/C1-609[»]
    ProteinModelPortaliP17169.
    SMRiP17169. Positions 2-609.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17169.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 218217Glutamine amidotransferase type-2Add
    BLAST
    Domaini286 – 426141SIS 1Add
    BLAST
    Domaini458 – 599142SIS 2Add
    BLAST

    Sequence similaritiesi

    Contains 2 SIS domains.Curated

    Keywords - Domaini

    Glutamine amidotransferase, Repeat

    Phylogenomic databases

    eggNOGiCOG0449.
    HOGENOMiHOG000258898.
    KOiK00820.
    OMAiPVTRRFM.
    OrthoDBiEOG6KT2Q1.
    PhylomeDBiP17169.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    HAMAPiMF_00164. GlmS.
    InterProiIPR017932. GATase_2_dom.
    IPR000583. GATase_dom.
    IPR005855. GlmS_trans.
    IPR029055. Ntn_hydrolases_N.
    IPR001347. SIS.
    [Graphical view]
    PANTHERiPTHR10937:SF0. PTHR10937:SF0. 1 hit.
    PfamiPF00310. GATase_2. 2 hits.
    PF01380. SIS. 2 hits.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR01135. glmS. 1 hit.
    PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
    PS51464. SIS. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P17169-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCGIVGAIAQ RDVAEILLEG LRRLEYRGYD SAGLAVVDAE GHMTRLRRLG    50
    KVQMLAQAAE EHPLHGGTGI AHTRWATHGE PSEVNAHPHV SEHIVVVHNG 100
    IIENHEPLRE ELKARGYTFV SETDTEVIAH LVNWELKQGG TLREAVLRAI 150
    PQLRGAYGTV IMDSRHPDTL LAARSGSPLV IGLGMGENFI ASDQLALLPV 200
    TRRFIFLEEG DIAEITRRSV NIFDKTGAEV KRQDIESNLQ YDAGDKGIYR 250
    HYMQKEIYEQ PNAIKNTLTG RISHGQVDLS ELGPNADELL SKVEHIQILA 300
    CGTSYNSGMV SRYWFESLAG IPCDVEIASE FRYRKSAVRR NSLMITLSQS 350
    GETADTLAGL RLSKELGYLG SLAICNVPGS SLVRESDLAL MTNAGTEIGV 400
    ASTKAFTTQL TVLLMLVAKL SRLKGLDASI EHDIVHGLQA LPSRIEQMLS 450
    QDKRIEALAE DFSDKHHALF LGRGDQYPIA LEGALKLKEI SYIHAEAYAA 500
    GELKHGPLAL IDADMPVIVV APNNELLEKL KSNIEEVRAR GGQLYVFADQ 550
    DAGFVSSDNM HIIEMPHVEE VIAPIFYTVP LQLLAYHVAL IKGTDVDQPR 600
    NLAKSVTVE 609
    Length:609
    Mass (Da):66,894
    Last modified:January 23, 2007 - v4
    Checksum:iA1CB929E839436E0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti419 – 4202KL → NV in CAA25785. (PubMed:6395859)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01631 Genomic DNA. Translation: CAA25785.1.
    L10328 Genomic DNA. Translation: AAA62080.1.
    U00096 Genomic DNA. Translation: AAC76752.1.
    AP009048 Genomic DNA. Translation: BAE77559.1.
    V00620 Genomic DNA. Translation: CAA23894.1.
    M18980 Genomic DNA. Translation: AAA23836.1.
    PIRiB65176. XNECGM.
    RefSeqiNP_418185.1. NC_000913.3.
    YP_491700.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76752; AAC76752; b3729.
    BAE77559; BAE77559; BAE77559.
    GeneIDi12933142.
    948241.
    KEGGiecj:Y75_p3439.
    eco:b3729.
    PATRICi32122955. VBIEscCol129921_3853.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01631 Genomic DNA. Translation: CAA25785.1 .
    L10328 Genomic DNA. Translation: AAA62080.1 .
    U00096 Genomic DNA. Translation: AAC76752.1 .
    AP009048 Genomic DNA. Translation: BAE77559.1 .
    V00620 Genomic DNA. Translation: CAA23894.1 .
    M18980 Genomic DNA. Translation: AAA23836.1 .
    PIRi B65176. XNECGM.
    RefSeqi NP_418185.1. NC_000913.3.
    YP_491700.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JXA X-ray 3.10 A/B/C 2-609 [» ]
    1MOQ X-ray 1.57 A 242-609 [» ]
    1MOR X-ray 1.90 A 242-609 [» ]
    1MOS X-ray 2.00 A 242-609 [» ]
    1XFF X-ray 1.80 A/B 2-241 [» ]
    1XFG X-ray 1.85 A/B 2-241 [» ]
    2J6H X-ray 2.35 A/B 2-609 [» ]
    2VF4 X-ray 2.95 X 2-609 [» ]
    2VF5 X-ray 2.90 X 2-609 [» ]
    3OOJ X-ray 2.50 A/B/C/D/E/F/G/H 3-609 [» ]
    4AMV X-ray 2.05 A/B/C 1-609 [» ]
    ProteinModelPortali P17169.
    SMRi P17169. Positions 2-609.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9775N.
    IntActi P17169. 8 interactions.
    MINTi MINT-1238536.
    STRINGi 511145.b3729.

    Proteomic databases

    PaxDbi P17169.
    PRIDEi P17169.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76752 ; AAC76752 ; b3729 .
    BAE77559 ; BAE77559 ; BAE77559 .
    GeneIDi 12933142.
    948241.
    KEGGi ecj:Y75_p3439.
    eco:b3729.
    PATRICi 32122955. VBIEscCol129921_3853.

    Organism-specific databases

    EchoBASEi EB0377.
    EcoGenei EG10382. glmS.

    Phylogenomic databases

    eggNOGi COG0449.
    HOGENOMi HOG000258898.
    KOi K00820.
    OMAi PVTRRFM.
    OrthoDBi EOG6KT2Q1.
    PhylomeDBi P17169.

    Enzyme and pathway databases

    BioCyci EcoCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER.
    ECOL316407:JW3707-MONOMER.
    MetaCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P17169.
    PROi P17169.

    Gene expression databases

    Genevestigatori P17169.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    HAMAPi MF_00164. GlmS.
    InterProi IPR017932. GATase_2_dom.
    IPR000583. GATase_dom.
    IPR005855. GlmS_trans.
    IPR029055. Ntn_hydrolases_N.
    IPR001347. SIS.
    [Graphical view ]
    PANTHERi PTHR10937:SF0. PTHR10937:SF0. 1 hit.
    Pfami PF00310. GATase_2. 2 hits.
    PF01380. SIS. 2 hits.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    TIGRFAMsi TIGR01135. glmS. 1 hit.
    PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
    PS51464. SIS. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS."
      Walker J.E., Gay N.J., Saraste M., Eberle A.N.
      Biochem. J. 224:799-815(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
      Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
      Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Possible involvement of Lys603 from Escherichia coli glucosamine-6-phosphate synthase in the binding of its substrate fructose 6-phosphate."
      Golinelli-Pimpaneau B., Badet B.
      Eur. J. Biochem. 201:175-182(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 49-52; 219-231; 489-493; 505-508 AND 601-609.
    6. "Unique insertion site of Tn7 in the E. coli chromosome."
      Lichtenstein C., Brenner S.
      Nature 297:601-603(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 490-609.
    7. "Insertion of transposon Tn7 into the Escherichia coli glmS transcriptional terminator."
      Gay N.J., Tybulewicz V.L.J., Walker J.E.
      Biochem. J. 234:111-117(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 607-609.
    8. "Sequence requirements of Escherichia coli attTn7, a specific site of transposon Tn7 insertion."
      McKown R.L., Orle K.A., Chen T., Craig N.L.
      J. Bacteriol. 170:352-358(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 597-609.
    9. "Molecular cloning and overexpression of the glucosamine synthetase gene from Escherichia coli."
      Dutka-Malen S., Mazodier P., Badet B.
      Biochimie 70:287-290(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    10. "Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8-A crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase."
      Isupov M.N., Obmolova G., Butterworth S., Badet-Denisot M.-A., Badet B., Polikarpov I., Littlechild J.A., Teplyakov A.
      Structure 4:801-810(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-241.
    11. "Involvement of the C-terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6-A crystal structure of the isomerase domain."
      Teplyakov A., Obmolova G., Badet-Denisot M.-A., Badet B., Polikarpov I.
      Structure 6:1047-1055(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 244-609.
    12. "The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate synthase."
      Teplyakov A., Obmolova G., Badet-Denisot M.-A., Badet B.
      Protein Sci. 8:596-602(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 242-609.

    Entry informationi

    Entry nameiGLMS_ECOLI
    AccessioniPrimary (citable) accession number: P17169
    Secondary accession number(s): P76745, Q2M847
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 156 of the entry and version 4 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. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    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