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P17169 (GLMS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:glmS
Ordered Locus Names:b3729, JW3707
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length609 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. HAMAP-Rule MF_00164

Catalytic activity

L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate. HAMAP-Rule MF_00164

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00164.

Sequence similarities

Contains 1 glutamine amidotransferase type-2 domain.

Contains 2 SIS domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ynbDP760933EBI-551022,EBI-551038

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_00164
Chain2 – 609608Glutamine--fructose-6-phosphate aminotransferase [isomerizing] HAMAP-Rule MF_00164
PRO_0000135328

Regions

Domain2 – 218217Glutamine amidotransferase type-2
Domain286 – 426141SIS 1
Domain458 – 599142SIS 2

Sites

Active site21Nucleophile; for GATase activity By similarity
Active site6041For Fru-6P isomerization activity

Experimental info

Sequence conflict419 – 4202KL → NV in CAA25785. Ref.1

Secondary structure

................................................................................................................. 609
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17169 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: A1CB929E839436E0

FASTA60966,894
        10         20         30         40         50         60 
MCGIVGAIAQ RDVAEILLEG LRRLEYRGYD SAGLAVVDAE GHMTRLRRLG KVQMLAQAAE 

        70         80         90        100        110        120 
EHPLHGGTGI AHTRWATHGE PSEVNAHPHV SEHIVVVHNG IIENHEPLRE ELKARGYTFV 

       130        140        150        160        170        180 
SETDTEVIAH LVNWELKQGG TLREAVLRAI PQLRGAYGTV IMDSRHPDTL LAARSGSPLV 

       190        200        210        220        230        240 
IGLGMGENFI ASDQLALLPV TRRFIFLEEG DIAEITRRSV NIFDKTGAEV KRQDIESNLQ 

       250        260        270        280        290        300 
YDAGDKGIYR HYMQKEIYEQ PNAIKNTLTG RISHGQVDLS ELGPNADELL SKVEHIQILA 

       310        320        330        340        350        360 
CGTSYNSGMV SRYWFESLAG IPCDVEIASE FRYRKSAVRR NSLMITLSQS GETADTLAGL 

       370        380        390        400        410        420 
RLSKELGYLG SLAICNVPGS SLVRESDLAL MTNAGTEIGV ASTKAFTTQL TVLLMLVAKL 

       430        440        450        460        470        480 
SRLKGLDASI EHDIVHGLQA LPSRIEQMLS QDKRIEALAE DFSDKHHALF LGRGDQYPIA 

       490        500        510        520        530        540 
LEGALKLKEI SYIHAEAYAA GELKHGPLAL IDADMPVIVV APNNELLEKL KSNIEEVRAR 

       550        560        570        580        590        600 
GGQLYVFADQ DAGFVSSDNM HIIEMPHVEE VIAPIFYTVP LQLLAYHVAL IKGTDVDQPR 


NLAKSVTVE 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRXNECGM. B65176.
RefSeqNP_418185.1. NC_000913.3.
YP_491700.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JXAX-ray3.10A/B/C2-608[»]
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[»]
ProteinModelPortalP17169.
SMRP17169. Positions 2-609.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9775N.
IntActP17169. 8 interactions.
MINTMINT-1238536.
STRING511145.b3729.

Proteomic databases

PaxDbP17169.
PRIDEP17169.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76752; AAC76752; b3729.
BAE77559; BAE77559; BAE77559.
GeneID12933142.
948241.
KEGGecj:Y75_p3439.
eco:b3729.
PATRIC32122955. VBIEscCol129921_3853.

Organism-specific databases

EchoBASEEB0377.
EcoGeneEG10382. glmS.

Phylogenomic databases

eggNOGCOG0449.
HOGENOMHOG000258898.
KOK00820.
OMALGIGENF.
OrthoDBEOG6KT2Q1.
PhylomeDBP17169.
ProtClustDBPRK00331.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP17169.

Family and domain databases

HAMAPMF_00164. GlmS.
InterProIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR001347. SIS.
[Graphical view]
PANTHERPTHR10937:SF0. PTHR10937:SF0. 1 hit.
PfamPF00310. GATase_2. 2 hits.
PF01380. SIS. 2 hits.
[Graphical view]
TIGRFAMsTIGR01135. glmS. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17169.
PROP17169.

Entry information

Entry nameGLMS_ECOLI
AccessionPrimary (citable) accession number: P17169
Secondary accession number(s): P76745, Q2M847
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 152 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene