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P17169

- GLMS_ECOLI

UniProt

P17169 - GLMS_ECOLI

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Protein

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

Gene

glmS

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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Nucleophile; for GATase activityBy 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

GO - Biological processi

  1. carbohydrate biosynthetic process Source: InterPro
  2. glutamine metabolic process Source: UniProtKB-HAMAP
  3. UDP-N-acetylglucosamine biosynthetic process Source: EcoCyc
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

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 – 11Removed
Chaini2 – 609608Glutamine--fructose-6-phosphate aminotransferase [isomerizing]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

1
609
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi14 – 2411Combined sources
Helixi25 – 273Combined sources
Beta strandi30 – 378Combined sources
Beta strandi43 – 508Combined sources
Helixi52 – 6110Combined sources
Beta strandi67 – 748Combined sources
Beta strandi77 – 793Combined sources
Turni83 – 853Combined sources
Beta strandi89 – 913Combined sources
Beta strandi94 – 1029Combined sources
Helixi105 – 11410Combined sources
Helixi125 – 13713Combined sources
Helixi142 – 1498Combined sources
Helixi150 – 1523Combined sources
Beta strandi155 – 1639Combined sources
Beta strandi170 – 1778Combined sources
Beta strandi180 – 1834Combined sources
Beta strandi188 – 1936Combined sources
Helixi194 – 1963Combined sources
Turni197 – 2004Combined sources
Beta strandi202 – 2065Combined sources
Beta strandi212 – 2154Combined sources
Beta strandi220 – 2234Combined sources
Beta strandi225 – 2273Combined sources
Beta strandi234 – 2363Combined sources
Turni241 – 2444Combined sources
Helixi252 – 2587Combined sources
Helixi260 – 2689Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi274 – 2774Combined sources
Helixi280 – 2823Combined sources
Helixi286 – 2927Combined sources
Beta strandi295 – 3006Combined sources
Helixi302 – 31817Combined sources
Beta strandi323 – 3275Combined sources
Helixi328 – 3325Combined sources
Beta strandi342 – 35110Combined sources
Helixi354 – 36310Combined sources
Turni364 – 3674Combined sources
Beta strandi369 – 3779Combined sources
Helixi381 – 3855Combined sources
Beta strandi386 – 3916Combined sources
Beta strandi399 – 4013Combined sources
Helixi404 – 42320Combined sources
Helixi428 – 44821Combined sources
Helixi449 – 4513Combined sources
Helixi454 – 4629Combined sources
Beta strandi466 – 4727Combined sources
Helixi474 – 4763Combined sources
Helixi477 – 49115Combined sources
Beta strandi494 – 4996Combined sources
Helixi500 – 5056Combined sources
Helixi507 – 5104Combined sources
Beta strandi517 – 5215Combined sources
Helixi524 – 53613Combined sources
Helixi537 – 5404Combined sources
Beta strandi544 – 5496Combined sources
Helixi550 – 5523Combined sources
Beta strandi560 – 5656Combined sources
Helixi570 – 5723Combined sources
Helixi573 – 59220Combined sources
Beta strandi596 – 5983Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP17169.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 2 SIS domains.Curated

Keywords - Domaini

Glutamine amidotransferase, Repeat

Phylogenomic databases

eggNOGiCOG0449.
HOGENOMiHOG000258898.
InParanoidiP17169.
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

        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti419 – 4202KL → NV in CAA25785. (PubMed:6395859)Curated

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.
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:
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 .
PIRi B65176. XNECGM.
RefSeqi NP_418185.1. NC_000913.3.
YP_491700.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

Chemistry

BindingDBi P17169.

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.
InParanoidi P17169.
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: November 26, 2014
This is version 158 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