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Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (EC 2.6.1.16) (D-fructose-6-phosphate amidotransferase) (GFAT) (Glucosamine-6-phosphate synthase) (Hexosephosphate aminotransferase) (L-glutamine--D-fructose-6-phosphate amidotransferase)

 GLMS_ECOLI              Reviewed;         609 AA.
P17169; P76745; Q2M847;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
28-MAR-2018, entry version 182.
RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing];
EC=2.6.1.16;
AltName: Full=D-fructose-6-phosphate amidotransferase;
AltName: Full=GFAT;
AltName: Full=Glucosamine-6-phosphate synthase;
AltName: Full=Hexosephosphate aminotransferase;
AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase;
Name=glmS; OrderedLocusNames=b3729, JW3707;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6395859; DOI=10.1042/bj2240799;
Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
"DNA sequence around the Escherichia coli unc operon. Completion of
the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS
and phoS.";
Biochem. J. 224:799-815(1984).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=7686882; DOI=10.1006/geno.1993.1230;
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
"DNA sequence and analysis of 136 kilobases of the Escherichia coli
genome: organizational symmetry around the origin of replication.";
Genomics 16:551-561(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 49-52; 219-231; 489-493; 505-508 AND 601-609.
PubMed=1915361; DOI=10.1111/j.1432-1033.1991.tb16271.x;
Golinelli-Pimpaneau B., Badet B.;
"Possible involvement of Lys603 from Escherichia coli glucosamine-6-
phosphate synthase in the binding of its substrate fructose 6-
phosphate.";
Eur. J. Biochem. 201:175-182(1991).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 490-609.
PubMed=6283361; DOI=10.1038/297601a0;
Lichtenstein C., Brenner S.;
"Unique insertion site of Tn7 in the E. coli chromosome.";
Nature 297:601-603(1982).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 607-609.
PubMed=3010949; DOI=10.1042/bj2340111;
Gay N.J., Tybulewicz V.L.J., Walker J.E.;
"Insertion of transposon Tn7 into the Escherichia coli glmS
transcriptional terminator.";
Biochem. J. 234:111-117(1986).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 597-609.
PubMed=2826397; DOI=10.1128/jb.170.1.352-358.1988;
McKown R.L., Orle K.A., Chen T., Craig N.L.;
"Sequence requirements of Escherichia coli attTn7, a specific site of
transposon Tn7 insertion.";
J. Bacteriol. 170:352-358(1988).
[9]
CHARACTERIZATION.
PubMed=3134953; DOI=10.1016/0300-9084(88)90073-9;
Dutka-Malen S., Mazodier P., Badet B.;
"Molecular cloning and overexpression of the glucosamine synthetase
gene from Escherichia coli.";
Biochimie 70:287-290(1988).
[10]
REGULATION BY THE GLMYZ CASCADE.
PubMed=18334534; DOI=10.1093/nar/gkn091;
Reichenbach B., Maes A., Kalamorz F., Hajnsdorf E., Goerke B.;
"The small RNA GlmY acts upstream of the sRNA GlmZ in the activation
of glmS expression and is subject to regulation by polyadenylation in
Escherichia coli.";
Nucleic Acids Res. 36:2570-2580(2008).
[11]
REGULATION BY THE GLMYZ CASCADE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=18351803; DOI=10.1371/journal.pbio.0060064;
Urban J.H., Vogel J.;
"Two seemingly homologous noncoding RNAs act hierarchically to
activate glmS mRNA translation.";
PLoS Biol. 6:E64-E64(2008).
[12]
REGULATION BY THE GLMYZ CASCADE.
PubMed=23475961; DOI=10.1101/gad.210112.112;
Gopel Y., Papenfort K., Reichenbach B., Vogel J., Gorke B.;
"Targeted decay of a regulatory small RNA by an adaptor protein for
RNase E and counteraction by an anti-adaptor RNA.";
Genes Dev. 27:552-564(2013).
[13]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-241.
PubMed=8805567; DOI=10.1016/S0969-2126(96)00087-1;
Isupov M.N., Obmolova G., Butterworth S., Badet-Denisot M.-A.,
Badet B., Polikarpov I., Littlechild J.A., Teplyakov A.;
"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.";
Structure 4:801-810(1996).
[14]
X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 244-609.
PubMed=9739095; DOI=10.1016/S0969-2126(98)00105-1;
Teplyakov A., Obmolova G., Badet-Denisot M.-A., Badet B.,
Polikarpov I.;
"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.";
Structure 6:1047-1055(1998).
[15]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 242-609.
PubMed=10091662; DOI=10.1110/ps.8.3.596;
Teplyakov A., Obmolova G., Badet-Denisot M.-A., Badet B.;
"The mechanism of sugar phosphate isomerization by glucosamine 6-
phosphate synthase.";
Protein Sci. 8:596-602(1999).
-!- FUNCTION: Catalyzes the first step in hexosamine metabolism,
converting fructose-6P into glucosamine-6P using glutamine as a
nitrogen source.
-!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L-
glutamate + D-glucosamine 6-phosphate.
-!- SUBUNIT: Homodimer.
-!- INTERACTION:
P62615:ispE; NbExp=2; IntAct=EBI-551022, EBI-562202;
P76093:ynbD; NbExp=4; IntAct=EBI-551022, EBI-551038;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- INDUCTION: Post-transcriptionally regulated by the GlmY/GlmZ sRNA
regulatory cascade. The sRNA GlmZ, together with Hfq, directly
activates glmS mRNA translation through base-pairing. A second
sRNA, GlmY, positively regulates glmS indirectly, by sequestering
the adapter protein RapZ and protecting GlmZ from RNA cleavage.
{ECO:0000269|PubMed:18334534, ECO:0000269|PubMed:18351803,
ECO:0000269|PubMed:23475961}.
-----------------------------------------------------------------------
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EMBL; X01631; CAA25785.1; -; Genomic_DNA.
EMBL; L10328; AAA62080.1; -; Genomic_DNA.
EMBL; U00096; AAC76752.1; -; Genomic_DNA.
EMBL; AP009048; BAE77559.1; -; Genomic_DNA.
EMBL; V00620; CAA23894.1; -; Genomic_DNA.
EMBL; M18980; AAA23836.1; -; Genomic_DNA.
PIR; B65176; XNECGM.
RefSeq; NP_418185.1; NC_000913.3.
RefSeq; WP_000334099.1; NZ_LN832404.1.
PDB; 1JXA; X-ray; 3.10 A; A/B/C=2-609.
PDB; 1MOQ; X-ray; 1.57 A; A=242-609.
PDB; 1MOR; X-ray; 1.90 A; A=242-609.
PDB; 1MOS; X-ray; 2.00 A; A=242-609.
PDB; 1XFF; X-ray; 1.80 A; A/B=2-241.
PDB; 1XFG; X-ray; 1.85 A; A/B=2-241.
PDB; 2J6H; X-ray; 2.35 A; A/B=2-609.
PDB; 2VF4; X-ray; 2.95 A; X=2-609.
PDB; 2VF5; X-ray; 2.90 A; X=2-609.
PDB; 3OOJ; X-ray; 2.50 A; A/B/C/D/E/F/G/H=3-609.
PDB; 4AMV; X-ray; 2.05 A; A/B/C=1-609.
PDBsum; 1JXA; -.
PDBsum; 1MOQ; -.
PDBsum; 1MOR; -.
PDBsum; 1MOS; -.
PDBsum; 1XFF; -.
PDBsum; 1XFG; -.
PDBsum; 2J6H; -.
PDBsum; 2VF4; -.
PDBsum; 2VF5; -.
PDBsum; 3OOJ; -.
PDBsum; 4AMV; -.
ProteinModelPortal; P17169; -.
SMR; P17169; -.
BioGrid; 4262136; 528.
DIP; DIP-9775N; -.
IntAct; P17169; 8.
STRING; 316407.85676309; -.
BindingDB; P17169; -.
DrugBank; DB03814; 2-(N-Morpholino)-Ethanesulfonic Acid.
DrugBank; DB02445; 2-Deoxy-2-Amino Glucitol-6-Phosphate.
DrugBank; DB02007; alpha-D-glucose 6-phosphate.
DrugBank; DB02657; Glucosamine 6-Phosphate.
DrugBank; DB03581; Glucose-6-Phosphate.
DrugBank; DB02446; Glutamine Hydroxamate.
EPD; P17169; -.
PaxDb; P17169; -.
PRIDE; P17169; -.
EnsemblBacteria; AAC76752; AAC76752; b3729.
EnsemblBacteria; BAE77559; BAE77559; BAE77559.
GeneID; 948241; -.
KEGG; ecj:JW3707; -.
KEGG; eco:b3729; -.
PATRIC; fig|1411691.4.peg.2971; -.
EchoBASE; EB0377; -.
EcoGene; EG10382; glmS.
eggNOG; ENOG4105C46; Bacteria.
eggNOG; COG0449; LUCA.
HOGENOM; HOG000258898; -.
InParanoid; P17169; -.
KO; K00820; -.
OMA; ASEYRYA; -.
PhylomeDB; P17169; -.
BioCyc; EcoCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER; -.
BioCyc; MetaCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER; -.
BRENDA; 2.6.1.16; 2026.
EvolutionaryTrace; P17169; -.
PRO; PR:P17169; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IDA:EcoCyc.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:EcoCyc.
CDD; cd05008; SIS_GlmS_GlmD_1; 1.
CDD; cd05009; SIS_GlmS_GlmD_2; 1.
Gene3D; 3.60.20.10; -; 1.
HAMAP; MF_00164; GlmS; 1.
InterPro; IPR017932; GATase_2_dom.
InterPro; IPR035466; GlmS/AgaS_SIS.
InterPro; IPR035490; GlmS/FrlB_SIS.
InterPro; IPR005855; GlmS_trans.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR001347; SIS.
PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
Pfam; PF01380; SIS; 2.
SUPFAM; SSF56235; SSF56235; 1.
TIGRFAMs; TIGR01135; glmS; 1.
PROSITE; PS51278; GATASE_TYPE_2; 1.
PROSITE; PS51464; SIS; 2.
1: Evidence at protein level;
3D-structure; Aminotransferase; Complete proteome; Cytoplasm;
Direct protein sequencing; Glutamine amidotransferase;
Reference proteome; Repeat; Transferase.
INIT_MET 1 1 Removed.
CHAIN 2 609 Glutamine--fructose-6-phosphate
aminotransferase [isomerizing].
/FTId=PRO_0000135328.
DOMAIN 2 218 Glutamine amidotransferase type-2.
DOMAIN 286 426 SIS 1.
DOMAIN 458 599 SIS 2.
ACT_SITE 2 2 Nucleophile; for GATase activity.
{ECO:0000250}.
ACT_SITE 604 604 For Fru-6P isomerization activity.
CONFLICT 419 420 KL -> NV (in Ref. 1; CAA25785).
{ECO:0000305}.
STRAND 3 8 {ECO:0000244|PDB:1XFF}.
HELIX 14 24 {ECO:0000244|PDB:1XFF}.
HELIX 25 27 {ECO:0000244|PDB:1XFF}.
STRAND 30 37 {ECO:0000244|PDB:1XFF}.
STRAND 43 50 {ECO:0000244|PDB:1XFF}.
HELIX 52 61 {ECO:0000244|PDB:1XFF}.
STRAND 67 74 {ECO:0000244|PDB:1XFF}.
STRAND 77 79 {ECO:0000244|PDB:1XFF}.
TURN 83 85 {ECO:0000244|PDB:1XFF}.
STRAND 89 91 {ECO:0000244|PDB:1XFF}.
STRAND 94 102 {ECO:0000244|PDB:1XFF}.
HELIX 105 114 {ECO:0000244|PDB:1XFF}.
HELIX 125 137 {ECO:0000244|PDB:1XFF}.
HELIX 142 149 {ECO:0000244|PDB:1XFF}.
HELIX 150 152 {ECO:0000244|PDB:1XFF}.
STRAND 155 163 {ECO:0000244|PDB:1XFF}.
STRAND 170 177 {ECO:0000244|PDB:1XFF}.
STRAND 180 183 {ECO:0000244|PDB:1XFF}.
STRAND 188 193 {ECO:0000244|PDB:1XFF}.
HELIX 194 196 {ECO:0000244|PDB:1XFF}.
TURN 197 200 {ECO:0000244|PDB:1XFF}.
STRAND 202 206 {ECO:0000244|PDB:1XFF}.
STRAND 212 215 {ECO:0000244|PDB:1XFF}.
STRAND 220 223 {ECO:0000244|PDB:1XFF}.
STRAND 225 227 {ECO:0000244|PDB:4AMV}.
STRAND 234 236 {ECO:0000244|PDB:1XFF}.
TURN 241 244 {ECO:0000244|PDB:4AMV}.
HELIX 252 258 {ECO:0000244|PDB:1MOQ}.
HELIX 260 268 {ECO:0000244|PDB:1MOQ}.
STRAND 271 273 {ECO:0000244|PDB:1MOQ}.
STRAND 274 277 {ECO:0000244|PDB:1MOR}.
HELIX 280 282 {ECO:0000244|PDB:1MOQ}.
HELIX 286 292 {ECO:0000244|PDB:1MOQ}.
STRAND 295 300 {ECO:0000244|PDB:1MOQ}.
HELIX 302 318 {ECO:0000244|PDB:1MOQ}.
STRAND 323 327 {ECO:0000244|PDB:1MOQ}.
HELIX 328 332 {ECO:0000244|PDB:1MOQ}.
STRAND 342 351 {ECO:0000244|PDB:1MOQ}.
HELIX 354 363 {ECO:0000244|PDB:1MOQ}.
TURN 364 367 {ECO:0000244|PDB:1MOQ}.
STRAND 369 377 {ECO:0000244|PDB:1MOQ}.
HELIX 381 385 {ECO:0000244|PDB:1MOQ}.
STRAND 386 391 {ECO:0000244|PDB:1MOQ}.
STRAND 399 401 {ECO:0000244|PDB:1MOQ}.
HELIX 404 423 {ECO:0000244|PDB:1MOQ}.
HELIX 428 448 {ECO:0000244|PDB:1MOQ}.
HELIX 449 451 {ECO:0000244|PDB:4AMV}.
HELIX 454 462 {ECO:0000244|PDB:1MOQ}.
STRAND 466 472 {ECO:0000244|PDB:1MOQ}.
HELIX 474 476 {ECO:0000244|PDB:1MOQ}.
HELIX 477 491 {ECO:0000244|PDB:1MOQ}.
STRAND 494 499 {ECO:0000244|PDB:1MOQ}.
HELIX 500 505 {ECO:0000244|PDB:1MOQ}.
HELIX 507 510 {ECO:0000244|PDB:1MOQ}.
STRAND 517 521 {ECO:0000244|PDB:1MOQ}.
HELIX 524 536 {ECO:0000244|PDB:1MOQ}.
HELIX 537 540 {ECO:0000244|PDB:1MOQ}.
STRAND 544 549 {ECO:0000244|PDB:1MOQ}.
HELIX 550 552 {ECO:0000244|PDB:1MOQ}.
STRAND 560 565 {ECO:0000244|PDB:1MOQ}.
HELIX 570 572 {ECO:0000244|PDB:1MOQ}.
HELIX 573 592 {ECO:0000244|PDB:1MOQ}.
STRAND 596 598 {ECO:0000244|PDB:1MOQ}.
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


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