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Protein

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

Gene

glmS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Active sitei2Nucleophile; for GATase activityBy similarity1
Active sitei604For Fru-6P isomerization activity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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.
BRENDAi2.6.1.16. 2026.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10382. glmS.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001353282 – 609Glutamine--fructose-6-phosphate aminotransferase [isomerizing]Add BLAST608

Proteomic databases

EPDiP17169.
PaxDbiP17169.
PRIDEiP17169.

Expressioni

Inductioni

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.3 Publications

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi4262136. 508 interactors.
DIPiDIP-9775N.
IntActiP17169. 8 interactors.
MINTiMINT-1238536.
STRINGi511145.b3729.

Chemistry databases

BindingDBiP17169.

Structurei

Secondary structure

1609
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Helixi14 – 24Combined sources11
Helixi25 – 27Combined sources3
Beta strandi30 – 37Combined sources8
Beta strandi43 – 50Combined sources8
Helixi52 – 61Combined sources10
Beta strandi67 – 74Combined sources8
Beta strandi77 – 79Combined sources3
Turni83 – 85Combined sources3
Beta strandi89 – 91Combined sources3
Beta strandi94 – 102Combined sources9
Helixi105 – 114Combined sources10
Helixi125 – 137Combined sources13
Helixi142 – 149Combined sources8
Helixi150 – 152Combined sources3
Beta strandi155 – 163Combined sources9
Beta strandi170 – 177Combined sources8
Beta strandi180 – 183Combined sources4
Beta strandi188 – 193Combined sources6
Helixi194 – 196Combined sources3
Turni197 – 200Combined sources4
Beta strandi202 – 206Combined sources5
Beta strandi212 – 215Combined sources4
Beta strandi220 – 223Combined sources4
Beta strandi225 – 227Combined sources3
Beta strandi234 – 236Combined sources3
Turni241 – 244Combined sources4
Helixi252 – 258Combined sources7
Helixi260 – 268Combined sources9
Beta strandi271 – 273Combined sources3
Beta strandi274 – 277Combined sources4
Helixi280 – 282Combined sources3
Helixi286 – 292Combined sources7
Beta strandi295 – 300Combined sources6
Helixi302 – 318Combined sources17
Beta strandi323 – 327Combined sources5
Helixi328 – 332Combined sources5
Beta strandi342 – 351Combined sources10
Helixi354 – 363Combined sources10
Turni364 – 367Combined sources4
Beta strandi369 – 377Combined sources9
Helixi381 – 385Combined sources5
Beta strandi386 – 391Combined sources6
Beta strandi399 – 401Combined sources3
Helixi404 – 423Combined sources20
Helixi428 – 448Combined sources21
Helixi449 – 451Combined sources3
Helixi454 – 462Combined sources9
Beta strandi466 – 472Combined sources7
Helixi474 – 476Combined sources3
Helixi477 – 491Combined sources15
Beta strandi494 – 499Combined sources6
Helixi500 – 505Combined sources6
Helixi507 – 510Combined sources4
Beta strandi517 – 521Combined sources5
Helixi524 – 536Combined sources13
Helixi537 – 540Combined sources4
Beta strandi544 – 549Combined sources6
Helixi550 – 552Combined sources3
Beta strandi560 – 565Combined sources6
Helixi570 – 572Combined sources3
Helixi573 – 592Combined sources20
Beta strandi596 – 598Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17169.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 218Glutamine amidotransferase type-2Add BLAST217
Domaini286 – 426SIS 1Add BLAST141
Domaini458 – 599SIS 2Add BLAST142

Sequence similaritiesi

Contains 2 SIS domains.Curated

Keywords - Domaini

Glutamine amidotransferase, Repeat

Phylogenomic databases

eggNOGiENOG4105C46. Bacteria.
COG0449. LUCA.
HOGENOMiHOG000258898.
InParanoidiP17169.
KOiK00820.
OMAiGEFFCAS.
PhylomeDBiP17169.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00164. GlmS. 1 hit.
InterProiIPR017932. GATase_2_dom.
IPR005855. GlmS_trans.
IPR029055. Ntn_hydrolases_N.
IPR001347. SIS.
[Graphical view]
PANTHERiPTHR10937:SF0. PTHR10937:SF0. 1 hit.
PfamiPF01380. 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

        10         20         30         40         50
MCGIVGAIAQ RDVAEILLEG LRRLEYRGYD SAGLAVVDAE GHMTRLRRLG
60 70 80 90 100
KVQMLAQAAE EHPLHGGTGI AHTRWATHGE PSEVNAHPHV SEHIVVVHNG
110 120 130 140 150
IIENHEPLRE ELKARGYTFV SETDTEVIAH LVNWELKQGG TLREAVLRAI
160 170 180 190 200
PQLRGAYGTV IMDSRHPDTL LAARSGSPLV IGLGMGENFI ASDQLALLPV
210 220 230 240 250
TRRFIFLEEG DIAEITRRSV NIFDKTGAEV KRQDIESNLQ YDAGDKGIYR
260 270 280 290 300
HYMQKEIYEQ PNAIKNTLTG RISHGQVDLS ELGPNADELL SKVEHIQILA
310 320 330 340 350
CGTSYNSGMV SRYWFESLAG IPCDVEIASE FRYRKSAVRR NSLMITLSQS
360 370 380 390 400
GETADTLAGL RLSKELGYLG SLAICNVPGS SLVRESDLAL MTNAGTEIGV
410 420 430 440 450
ASTKAFTTQL TVLLMLVAKL SRLKGLDASI EHDIVHGLQA LPSRIEQMLS
460 470 480 490 500
QDKRIEALAE DFSDKHHALF LGRGDQYPIA LEGALKLKEI SYIHAEAYAA
510 520 530 540 550
GELKHGPLAL IDADMPVIVV APNNELLEKL KSNIEEVRAR GGQLYVFADQ
560 570 580 590 600
DAGFVSSDNM HIIEMPHVEE VIAPIFYTVP LQLLAYHVAL IKGTDVDQPR

NLAKSVTVE
Length:609
Mass (Da):66,894
Last modified:January 23, 2007 - v4
Checksum:iA1CB929E839436E0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti419 – 420KL → NV in CAA25785 (PubMed:6395859).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000334099.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76752; AAC76752; b3729.
BAE77559; BAE77559; BAE77559.
GeneIDi948241.
KEGGiecj:JW3707.
eco:b3729.
PATRICi32122955. VBIEscCol129921_3853.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000334099.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262136. 508 interactors.
DIPiDIP-9775N.
IntActiP17169. 8 interactors.
MINTiMINT-1238536.
STRINGi511145.b3729.

Chemistry databases

BindingDBiP17169.

Proteomic databases

EPDiP17169.
PaxDbiP17169.
PRIDEiP17169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76752; AAC76752; b3729.
BAE77559; BAE77559; BAE77559.
GeneIDi948241.
KEGGiecj:JW3707.
eco:b3729.
PATRICi32122955. VBIEscCol129921_3853.

Organism-specific databases

EchoBASEiEB0377.
EcoGeneiEG10382. glmS.

Phylogenomic databases

eggNOGiENOG4105C46. Bacteria.
COG0449. LUCA.
HOGENOMiHOG000258898.
InParanoidiP17169.
KOiK00820.
OMAiGEFFCAS.
PhylomeDBiP17169.

Enzyme and pathway databases

BioCyciEcoCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER.
ECOL316407:JW3707-MONOMER.
MetaCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER.
BRENDAi2.6.1.16. 2026.

Miscellaneous databases

EvolutionaryTraceiP17169.
PROiP17169.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00164. GlmS. 1 hit.
InterProiIPR017932. GATase_2_dom.
IPR005855. GlmS_trans.
IPR029055. Ntn_hydrolases_N.
IPR001347. SIS.
[Graphical view]
PANTHERiPTHR10937:SF0. PTHR10937:SF0. 1 hit.
PfamiPF01380. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 173 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

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.