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P17169

- GLMS_ECOLI

UniProt

P17169 - GLMS_ECOLI

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Protein
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]
Gene
glmS, b3729, JW3707
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Nucleophile; for GATase activity By 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. UDP-N-acetylglucosamine biosynthetic process Source: EcoCyc
  2. carbohydrate biosynthetic process Source: InterPro
  3. glutamine metabolic process Source: UniProtKB-HAMAP
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.

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

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 609608Glutamine--fructose-6-phosphate aminotransferase [isomerizing]UniRule annotation
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

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.

Miscellaneous databases

EvolutionaryTraceiP17169.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 2 SIS domains.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti419 – 4202KL → NV in CAA25785. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 155 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

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