P17169 (GLMS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	glmS
Ordered Locus Names:	b3729, JW3707

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	609 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Glutamine amidotransferase Repeat
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	UDP-N-acetylglucosamine biosynthetic process Inferred from mutant phenotype PubMed 5541523. Source: EcoCyc carbohydrate biosynthetic process Inferred from electronic annotation. Source: InterPro glutamine metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro glutamine-fructose-6-phosphate transaminase (isomerizing) activity Inferred from direct assay PubMed 3297136. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ispE	P62615	1	EBI-551022,EBI-562202
ynbD	P76093	1	EBI-551022,EBI-551038

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed HAMAP-Rule MF_00164

Chain

2 – 609

608

Glutamine--fructose-6-phosphate aminotransferase [isomerizing] HAMAP-Rule MF_00164

PRO_0000135328

Regions

Domain

2 – 218

217

Glutamine amidotransferase type-2

Domain

286 – 426

141

SIS 1

Domain

458 – 599

142

SIS 2

Sites

Active site

2

1

Nucleophile; for GATase activity By similarity

Active site

604

1

For Fru-6P isomerization activity

Experimental info

Sequence conflict

419 – 420

2

KL → NV in CAA25785. Ref.1

Secondary structure

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609

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

14 – 24

11

Helix

25 – 27

3

Beta strand

30 – 37

8

Beta strand

43 – 50

8

Helix

52 – 61

10

Beta strand

67 – 74

8

Beta strand

77 – 79

3

Turn

83 – 85

3

Beta strand

89 – 91

3

Beta strand

94 – 102

9

Helix

105 – 114

10

Helix

125 – 137

13

Helix

142 – 149

8

Helix

150 – 152

3

Beta strand

155 – 163

9

Beta strand

170 – 177

8

Beta strand

180 – 183

4

Beta strand

188 – 193

6

Helix

194 – 196

3

Turn

197 – 200

4

Beta strand

202 – 206

5

Beta strand

212 – 215

4

Beta strand

220 – 223

4

Beta strand

225 – 227

3

Beta strand

234 – 236

3

Turn

241 – 244

4

Helix

252 – 258

7

Helix

260 – 268

9

Beta strand

271 – 273

3

Beta strand

274 – 277

4

Helix

280 – 282

3

Helix

286 – 292

7

Beta strand

295 – 300

6

Helix

302 – 318

17

Beta strand

323 – 327

5

Helix

328 – 332

5

Beta strand

342 – 351

10

Helix

354 – 363

10

Turn

364 – 367

4

Beta strand

369 – 377

9

Helix

381 – 385

5

Beta strand

386 – 391

6

Beta strand

399 – 401

3

Helix

404 – 423

20

Helix

428 – 448

21

Helix

449 – 451

3

Helix

454 – 462

9

Beta strand

466 – 472

7

Helix

474 – 476

3

Helix

477 – 491

15

Beta strand

494 – 499

6

Helix

500 – 505

6

Helix

507 – 510

4

Beta strand

517 – 521

5

Helix

524 – 536

13

Helix

537 – 540

4

Beta strand

544 – 549

6

Helix

550 – 552

3

Beta strand

560 – 565

6

Helix

570 – 572

3

Helix

573 – 592

20

Beta strand

596 – 598

3

Sequences

	Sequence		Length	Mass (Da)
	P17169 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: A1CB929E839436E0	FASTA	609	66,894
	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

References

	« Hide 'large scale' referencesShow '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 277:1453-1474(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.

PIR

XNECGM. B65176.

RefSeq

NP_418185.1. NC_000913.2.
YP_491700.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JXA	X-ray	3.10	A/B/C	2-608	[»]
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	[»]
2BPL	X-ray	2.05	A/B/C	2-608	[»]
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	[»]

ProteinModelPortal

P17169.

SMR

P17169. Positions 2-609.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9775N.

IntAct

P17169. 8 interactions.

MINT

MINT-1238536.

STRING

511145.b3729.

Proteomic databases

PaxDb

P17169.

PRIDE

P17169.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76752; AAC76752; b3729.
BAE77559; BAE77559; BAE77559.

GeneID

12933142.
948241.

KEGG

ecj:Y75_p3439.
eco:b3729.

PATRIC

32122955. VBIEscCol129921_3853.

Organism-specific databases

EchoBASE

EB0377.

EcoGene

EG10382. glmS.

Phylogenomic databases

eggNOG

COG0449.

HOGENOM

HOG000258898.

KO

K00820.

OMA

HLVHWEL.

ProtClustDB

PRK00331.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P17169.

Family and domain databases

HAMAP

MF_00164. GlmS.

InterPro

IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR001347. SIS.
[Graphical view]

PANTHER

PTHR10937:SF0. PTHR10937:SF0. 1 hit.

Pfam

PF00310. GATase_2. 2 hits.
PF01380. SIS. 2 hits.
[Graphical view]

TIGRFAMs

TIGR01135. glmS. 1 hit.

PROSITE

PS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P17169.

Entry information

Entry name

GLMS_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 144 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program