GLMS_ECOLI
ID GLMS_ECOLI Reviewed; 609 AA.
AC P17169; P76745; Q2M847;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing];
DE EC=2.6.1.16;
DE AltName: Full=D-fructose-6-phosphate amidotransferase;
DE AltName: Full=GFAT;
DE AltName: Full=Glucosamine-6-phosphate synthase;
DE AltName: Full=Hexosephosphate aminotransferase;
DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase;
GN Name=glmS; OrderedLocusNames=b3729, JW3707;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6395859; DOI=10.1042/bj2240799;
RA Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
RT "DNA sequence around the Escherichia coli unc operon. Completion of the
RT sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and
RT phoS.";
RL Biochem. J. 224:799-815(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 49-52; 219-231; 489-493; 505-508 AND 601-609.
RX PubMed=1915361; DOI=10.1111/j.1432-1033.1991.tb16271.x;
RA Golinelli-Pimpaneau B., Badet B.;
RT "Possible involvement of Lys603 from Escherichia coli glucosamine-6-
RT phosphate synthase in the binding of its substrate fructose 6-phosphate.";
RL Eur. J. Biochem. 201:175-182(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 490-609.
RX PubMed=6283361; DOI=10.1038/297601a0;
RA Lichtenstein C., Brenner S.;
RT "Unique insertion site of Tn7 in the E. coli chromosome.";
RL Nature 297:601-603(1982).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 607-609.
RX PubMed=3010949; DOI=10.1042/bj2340111;
RA Gay N.J., Tybulewicz V.L.J., Walker J.E.;
RT "Insertion of transposon Tn7 into the Escherichia coli glmS transcriptional
RT terminator.";
RL Biochem. J. 234:111-117(1986).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 597-609.
RX PubMed=2826397; DOI=10.1128/jb.170.1.352-358.1988;
RA McKown R.L., Orle K.A., Chen T., Craig N.L.;
RT "Sequence requirements of Escherichia coli attTn7, a specific site of
RT transposon Tn7 insertion.";
RL J. Bacteriol. 170:352-358(1988).
RN [9]
RP CHARACTERIZATION.
RX PubMed=3134953; DOI=10.1016/0300-9084(88)90073-9;
RA Dutka-Malen S., Mazodier P., Badet B.;
RT "Molecular cloning and overexpression of the glucosamine synthetase gene
RT from Escherichia coli.";
RL Biochimie 70:287-290(1988).
RN [10]
RP REGULATION BY THE GLMYZ CASCADE.
RX PubMed=18334534; DOI=10.1093/nar/gkn091;
RA Reichenbach B., Maes A., Kalamorz F., Hajnsdorf E., Goerke B.;
RT "The small RNA GlmY acts upstream of the sRNA GlmZ in the activation of
RT glmS expression and is subject to regulation by polyadenylation in
RT Escherichia coli.";
RL Nucleic Acids Res. 36:2570-2580(2008).
RN [11]
RP REGULATION BY THE GLMYZ CASCADE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=18351803; DOI=10.1371/journal.pbio.0060064;
RA Urban J.H., Vogel J.;
RT "Two seemingly homologous noncoding RNAs act hierarchically to activate
RT glmS mRNA translation.";
RL PLoS Biol. 6:E64-E64(2008).
RN [12]
RP REGULATION BY THE GLMYZ CASCADE.
RX PubMed=23475961; DOI=10.1101/gad.210112.112;
RA Gopel Y., Papenfort K., Reichenbach B., Vogel J., Gorke B.;
RT "Targeted decay of a regulatory small RNA by an adaptor protein for RNase E
RT and counteraction by an anti-adaptor RNA.";
RL Genes Dev. 27:552-564(2013).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-241.
RX PubMed=8805567; DOI=10.1016/s0969-2126(96)00087-1;
RA Isupov M.N., Obmolova G., Butterworth S., Badet-Denisot M.-A., Badet B.,
RA Polikarpov I., Littlechild J.A., Teplyakov A.;
RT "Substrate binding is required for assembly of the active conformation of
RT the catalytic site in Ntn amidotransferases: evidence from the 1.8-A
RT crystal structure of the glutaminase domain of glucosamine 6-phosphate
RT synthase.";
RL Structure 4:801-810(1996).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 244-609.
RX PubMed=9739095; DOI=10.1016/s0969-2126(98)00105-1;
RA Teplyakov A., Obmolova G., Badet-Denisot M.-A., Badet B., Polikarpov I.;
RT "Involvement of the C-terminus in intramolecular nitrogen channeling in
RT glucosamine 6-phosphate synthase: evidence from a 1.6-A crystal structure
RT of the isomerase domain.";
RL Structure 6:1047-1055(1998).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 242-609.
RX PubMed=10091662; DOI=10.1110/ps.8.3.596;
RA Teplyakov A., Obmolova G., Badet-Denisot M.-A., Badet B.;
RT "The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate
RT synthase.";
RL Protein Sci. 8:596-602(1999).
CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P17169; P62615: ispE; NbExp=2; IntAct=EBI-551022, EBI-562202;
CC P17169; P76093: ynbD; NbExp=4; IntAct=EBI-551022, EBI-551038;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Post-transcriptionally regulated by the GlmY/GlmZ sRNA
CC regulatory cascade. The sRNA GlmZ, together with Hfq, directly
CC activates glmS mRNA translation through base-pairing. A second sRNA,
CC GlmY, positively regulates glmS indirectly, by sequestering the adapter
CC protein RapZ and protecting GlmZ from RNA cleavage.
CC {ECO:0000269|PubMed:18334534, ECO:0000269|PubMed:18351803,
CC ECO:0000269|PubMed:23475961}.
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DR EMBL; X01631; CAA25785.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62080.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76752.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77559.1; -; Genomic_DNA.
DR EMBL; V00620; CAA23894.1; -; Genomic_DNA.
DR EMBL; M18980; AAA23836.1; -; Genomic_DNA.
DR PIR; B65176; XNECGM.
DR RefSeq; NP_418185.1; NC_000913.3.
DR RefSeq; WP_000334099.1; NZ_SSZK01000036.1.
DR PDB; 1JXA; X-ray; 3.10 A; A/B/C=2-609.
DR PDB; 1MOQ; X-ray; 1.57 A; A=242-609.
DR PDB; 1MOR; X-ray; 1.90 A; A=242-609.
DR PDB; 1MOS; X-ray; 2.00 A; A=242-609.
DR PDB; 1XFF; X-ray; 1.80 A; A/B=2-241.
DR PDB; 1XFG; X-ray; 1.85 A; A/B=2-241.
DR PDB; 2J6H; X-ray; 2.35 A; A/B=2-609.
DR PDB; 2VF4; X-ray; 2.95 A; X=2-609.
DR PDB; 2VF5; X-ray; 2.90 A; X=2-609.
DR PDB; 3OOJ; X-ray; 2.50 A; A/B/C/D/E/F/G/H=3-609.
DR PDB; 4AMV; X-ray; 2.05 A; A/B/C=1-609.
DR PDB; 7DNR; X-ray; 1.70 A; A/B=242-609.
DR PDBsum; 1JXA; -.
DR PDBsum; 1MOQ; -.
DR PDBsum; 1MOR; -.
DR PDBsum; 1MOS; -.
DR PDBsum; 1XFF; -.
DR PDBsum; 1XFG; -.
DR PDBsum; 2J6H; -.
DR PDBsum; 2VF4; -.
DR PDBsum; 2VF5; -.
DR PDBsum; 3OOJ; -.
DR PDBsum; 4AMV; -.
DR PDBsum; 7DNR; -.
DR AlphaFoldDB; P17169; -.
DR SMR; P17169; -.
DR BioGRID; 4262136; 528.
DR BioGRID; 852543; 1.
DR DIP; DIP-9775N; -.
DR IntAct; P17169; 8.
DR STRING; 511145.b3729; -.
DR BindingDB; P17169; -.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR DrugBank; DB02445; 2-Deoxy-2-Amino Glucitol-6-Phosphate.
DR DrugBank; DB02007; alpha-D-glucose 6-phosphate.
DR DrugBank; DB02657; Glucosamine 6-Phosphate.
DR DrugBank; DB03581; Glucose-6-Phosphate.
DR DrugBank; DB02446; Glutamine hydroxamate.
DR MEROPS; C44.971; -.
DR jPOST; P17169; -.
DR PaxDb; P17169; -.
DR PRIDE; P17169; -.
DR EnsemblBacteria; AAC76752; AAC76752; b3729.
DR EnsemblBacteria; BAE77559; BAE77559; BAE77559.
DR GeneID; 66672367; -.
DR GeneID; 948241; -.
DR KEGG; ecj:JW3707; -.
DR KEGG; eco:b3729; -.
DR PATRIC; fig|1411691.4.peg.2971; -.
DR EchoBASE; EB0377; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_6; -.
DR InParanoid; P17169; -.
DR OMA; ASEYRYA; -.
DR PhylomeDB; P17169; -.
DR BioCyc; EcoCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MON; -.
DR BioCyc; MetaCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MON; -.
DR BRENDA; 2.6.1.16; 2026.
DR SABIO-RK; P17169; -.
DR EvolutionaryTrace; P17169; -.
DR PRO; PR:P17169; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IDA:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:EcoCyc.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_00164; GlmS; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR005855; GlmS_trans.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01135; glmS; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Cytoplasm; Direct protein sequencing;
KW Glutamine amidotransferase; Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..609
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing]"
FT /id="PRO_0000135328"
FT DOMAIN 2..218
FT /note="Glutamine amidotransferase type-2"
FT DOMAIN 286..426
FT /note="SIS 1"
FT DOMAIN 458..599
FT /note="SIS 2"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 604
FT /note="For Fru-6P isomerization activity"
FT CONFLICT 419..420
FT /note="KL -> NV (in Ref. 1; CAA25785)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1XFF"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:1XFF"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1XFF"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1XFF"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:1XFF"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:1XFF"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:1XFF"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1XFF"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1XFF"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1XFF"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:1XFF"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:1XFF"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:1XFF"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:1XFF"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1XFF"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:1XFF"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:1XFF"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1XFF"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:1XFF"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1XFF"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:1XFF"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:1XFF"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:1XFF"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1XFF"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:4AMV"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1XFF"
FT TURN 241..244
FT /evidence="ECO:0007829|PDB:4AMV"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:1MOQ"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:1MOQ"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:1MOR"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:1MOQ"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 302..318
FT /evidence="ECO:0007829|PDB:1MOQ"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 328..332
FT /evidence="ECO:0007829|PDB:1MOQ"
FT STRAND 342..351
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 354..363
FT /evidence="ECO:0007829|PDB:1MOQ"
FT TURN 364..367
FT /evidence="ECO:0007829|PDB:1MOQ"
FT STRAND 369..377
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 381..385
FT /evidence="ECO:0007829|PDB:1MOQ"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:1MOQ"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 404..423
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 428..448
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:4AMV"
FT HELIX 454..462
FT /evidence="ECO:0007829|PDB:1MOQ"
FT STRAND 466..472
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 477..491
FT /evidence="ECO:0007829|PDB:1MOQ"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 500..505
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 507..510
FT /evidence="ECO:0007829|PDB:1MOQ"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 524..536
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 537..540
FT /evidence="ECO:0007829|PDB:1MOQ"
FT STRAND 544..549
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:1MOQ"
FT STRAND 560..565
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:1MOQ"
FT HELIX 573..592
FT /evidence="ECO:0007829|PDB:1MOQ"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:1MOQ"
SQ SEQUENCE 609 AA; 66894 MW; A1CB929E839436E0 CRC64;
MCGIVGAIAQ RDVAEILLEG LRRLEYRGYD SAGLAVVDAE GHMTRLRRLG KVQMLAQAAE
EHPLHGGTGI AHTRWATHGE PSEVNAHPHV SEHIVVVHNG IIENHEPLRE ELKARGYTFV
SETDTEVIAH LVNWELKQGG TLREAVLRAI PQLRGAYGTV IMDSRHPDTL LAARSGSPLV
IGLGMGENFI ASDQLALLPV TRRFIFLEEG DIAEITRRSV NIFDKTGAEV KRQDIESNLQ
YDAGDKGIYR HYMQKEIYEQ PNAIKNTLTG RISHGQVDLS ELGPNADELL SKVEHIQILA
CGTSYNSGMV SRYWFESLAG IPCDVEIASE FRYRKSAVRR NSLMITLSQS GETADTLAGL
RLSKELGYLG SLAICNVPGS SLVRESDLAL MTNAGTEIGV ASTKAFTTQL TVLLMLVAKL
SRLKGLDASI EHDIVHGLQA LPSRIEQMLS QDKRIEALAE DFSDKHHALF LGRGDQYPIA
LEGALKLKEI SYIHAEAYAA GELKHGPLAL IDADMPVIVV APNNELLEKL KSNIEEVRAR
GGQLYVFADQ DAGFVSSDNM HIIEMPHVEE VIAPIFYTVP LQLLAYHVAL IKGTDVDQPR
NLAKSVTVE
