ID GLMS_ECOLI STANDARD; PRT; 608 AA. AC P17169; P76745; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 3. DT 07-FEB-2006, entry version 68. DE Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] DE (EC 2.6.1.16) (Hexosephosphate aminotransferase) (D-fructose-6- DE phosphate amidotransferase) (GFAT) (L-glutamine-D-fructose-6-phosphate DE amidotransferase) (Glucosamine-6-phosphate synthase). GN Name=glmS; OrderedLocusNames=b3729; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=85121806; PubMed=6395859; RA Walker J.E., Gay N.J., Saraste M., Eberle A.N.; RT "DNA sequence around the Escherichia coli unc operon. Completion of RT the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS RT and phoS."; RL Biochem. J. 224:799-815(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12 / MG1655; RX MEDLINE=93315143; PubMed=7686882; RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.; RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli RT genome: organizational symmetry around the origin of replication."; RL Genomics 16:551-561(1993). RN [3] RP PROTEIN SEQUENCE OF 48-51; 218-230; 488-492; 504-507 AND 600-608. RX MEDLINE=92007872; PubMed=1915361; RA Golinelli-Pimpaneau B., Badet B.; RT "Possible involvement of Lys603 from Escherichia coli glucosamine-6- RT phosphate synthase in the binding of its substrate fructose 6- RT phosphate."; RL Eur. J. Biochem. 201:175-182(1991). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 489-608. RX MEDLINE=82220022; PubMed=6283361; RA Lichtenstein C., Brenner S.; RT "Unique insertion site of Tn7 in the E. coli chromosome."; RL Nature 297:601-603(1982). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 606-608. RX MEDLINE=86215091; PubMed=3010949; RA Gay N.J., Tybulewicz V.L.J., Walker J.E.; RT "Insertion of transposon Tn7 into the Escherichia coli glmS RT transcriptional terminator."; RL Biochem. J. 234:111-117(1986). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 596-608. RX MEDLINE=88086894; PubMed=2826397; RA McKown R.L., Orle K.A., Chen T., Craig N.L.; RT "Sequence requirements of Escherichia coli attTn7, a specific site of RT transposon Tn7 insertion."; RL J. Bacteriol. 170:352-358(1988). RN [7] RP CHARACTERIZATION. RX MEDLINE=88281539; PubMed=3134953; DOI=10.1016/0300-9084(88)90073-9; RA Dutka-Malen S., Mazodier P., Badet B.; RT "Molecular cloning and overexpression of the glucosamine synthetase RT gene from Escherichia coli."; RL Biochimie 70:287-290(1988). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-240. RX MEDLINE=96434326; PubMed=8805567; DOI=10.1016/S0969-2126(96)00087-1; RA Isupov M.N., Obmolova G., Butterworth S., Badet-Denisot M.-A., RA Badet B., Polikarpov I., Littlechild J.A., Teplyakov A.; RT "Substrate binding is required for assembly of the active conformation RT of the catalytic site in Ntn amidotransferases: evidence from the 1.8- RT A crystal structure of the glutaminase domain of glucosamine 6- RT phosphate synthase."; RL Structure 4:801-810(1996). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 243-608. RX MEDLINE=98416699; PubMed=9739095; DOI=10.1016/S0969-2126(98)00105-1; RA Teplyakov A., Obmolova G., Badet-Denisot M.-A., Badet B., RA Polikarpov I.; RT "Involvement of the C terminus in intramolecular nitrogen channeling RT in glucosamine 6-phosphate synthase: evidence from a 1.6-A crystal RT structure of the isomerase domain."; RL Structure 6:1047-1055(1998). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 241-608. RX MEDLINE=99190083; PubMed=10091662; RA Teplyakov A., Obmolova G., Badet-Denisot M.A., Badet B.; RT "The mechanism of sugar phosphate isomerization by glucosamine 6- RT phosphate synthase."; RL Protein Sci. 8:596-602(1999). CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, CC converting fructose-6P into glucosamine-6P using glutamine as a CC nitrogen source. CC -!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L- CC glutamate + D-glucosamine 6-phosphate. CC -!- SUBUNIT: Homodimer. CC -!- INTERACTION: CC P00957:alaS; NbExp=1; IntAct=EBI-551022, EBI-544061; CC P08622:dnaJ; NbExp=1; IntAct=EBI-551022, EBI-545285; CC P76552:eutH; NbExp=1; IntAct=EBI-551022, EBI-551031; CC P62615:ispE; NbExp=1; IntAct=EBI-551022, EBI-562202; CC P61175:rplV; NbExp=1; IntAct=EBI-551022, EBI-542255; CC P21166:trkH; NbExp=1; IntAct=EBI-551022, EBI-550268; CC P76093:ynbD; NbExp=1; IntAct=EBI-551022, EBI-551038; CC P33366:yohD; NbExp=1; IntAct=EBI-551022, EBI-551046; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: In the C-terminal section; belongs to the SIS family. CC GFAT subfamily. CC -!- SIMILARITY: Contains 1 type-2 glutamine amidotransferase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X01631; CAA25785.1; -; Genomic_DNA. DR EMBL; L10328; AAA62080.1; -; Genomic_DNA. DR EMBL; U00096; AAC76752.1; -; Genomic_DNA. DR EMBL; V00620; CAA23894.1; -; Genomic_DNA. DR EMBL; M18980; AAA23836.1; -; Genomic_DNA. DR PIR; B65176; XNECGM. DR PDB; 1JXA; X-ray; A/B/C=1-608. DR PDB; 1MOQ; X-ray; @=241-608. DR PDB; 1MOR; X-ray; @=241-608. DR PDB; 1MOS; X-ray; A=241-608. DR PDB; 1XFF; X-ray; A/B=1-240. DR PDB; 1XFG; X-ray; A/B=1-240. DR MEROPS; C44.971; -. DR EchoBASE; EB0377; -. DR EcoGene; EG10382; glmS. DR BioCyc; EcoCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER; -. DR GO; GO:0005515; F:protein binding; IPI. DR HAMAP; MF_00164; -; 1. DR InterPro; IPR000583; GATase_2. DR InterPro; IPR005855; GlmS_trans. DR InterPro; IPR001347; SIS. DR Pfam; PF00310; GATase_2; 1. DR Pfam; PF01380; SIS; 2. DR TIGRFAMs; TIGR01135; glmS; 1. DR PROSITE; PS00443; GATASE_TYPE_II; 1. KW 3D-structure; Aminotransferase; Complete proteome; KW Direct protein sequencing; Glutamine amidotransferase; Transferase. FT INIT_MET 0 0 FT CHAIN 1 608 Glucosamine--fructose-6-phosphate FT aminotransferase [isomerizing]. FT /FTId=PRO_0000135328. FT REGION 1 181 Glutamine amidotransferase. FT ACT_SITE 1 1 GATase. FT ACT_SITE 603 603 Isomerization Fru-6P. FT CONFLICT 418 419 KL -> NV (in Ref. 1). FT STRAND 2 2 FT STRAND 4 7 FT HELIX 13 21 FT TURN 22 23 FT TURN 25 26 FT STRAND 30 31 FT STRAND 34 36 FT STRAND 42 44 FT STRAND 47 48 FT HELIX 51 59 FT TURN 60 60 FT STRAND 67 69 FT STRAND 72 72 FT TURN 81 83 FT STRAND 88 90 FT TURN 91 92 FT STRAND 93 95 FT STRAND 100 101 FT TURN 102 105 FT HELIX 106 113 FT HELIX 124 136 FT TURN 137 137 FT HELIX 141 148 FT HELIX 149 151 FT STRAND 154 156 FT STRAND 159 162 FT TURN 163 164 FT TURN 166 167 FT STRAND 169 171 FT STRAND 174 174 FT STRAND 179 182 FT STRAND 187 190 FT TURN 193 194 FT STRAND 202 205 FT STRAND 213 215 FT TURN 216 217 FT STRAND 218 222 FT STRAND 228 229 FT STRAND 234 235 FT TURN 238 239 FT TURN 242 243 FT TURN 246 247 FT HELIX 251 266 FT TURN 267 267 FT HELIX 279 281 FT TURN 286 288 FT HELIX 289 291 FT STRAND 294 298 FT HELIX 301 316 FT TURN 317 318 FT STRAND 322 323 FT HELIX 327 330 FT TURN 331 332 FT STRAND 341 345 FT HELIX 353 364 FT TURN 365 366 FT STRAND 372 374 FT HELIX 380 384 FT STRAND 389 390 FT HELIX 403 422 FT TURN 423 424 FT HELIX 427 437 FT TURN 438 439 FT HELIX 441 448 FT TURN 449 450 FT HELIX 451 459 FT TURN 460 461 FT STRAND 466 471 FT TURN 474 475 FT HELIX 476 490 FT STRAND 493 498 FT HELIX 499 504 FT TURN 505 505 FT HELIX 506 508 FT TURN 509 509 FT TURN 512 513 FT STRAND 515 520 FT TURN 524 525 FT HELIX 526 537 FT TURN 538 539 FT STRAND 542 548 FT TURN 549 550 FT STRAND 559 561 FT STRAND 564 564 FT TURN 570 571 FT HELIX 572 591 FT TURN 592 592 FT TURN 599 600 SQ SEQUENCE 608 AA; 66763 MW; 899EDA38B6F77149 CRC64; CGIVGAIAQR DVAEILLEGL RRLEYRGYDS AGLAVVDAEG HMTRLRRLGK VQMLAQAAEE HPLHGGTGIA HTRWATHGEP SEVNAHPHVS EHIVVVHNGI IENHEPLREE LKARGYTFVS ETDTEVIAHL VNWELKQGGT LREAVLRAIP QLRGAYGTVI MDSRHPDTLL AARSGSPLVI GLGMGENFIA SDQLALLPVT RRFIFLEEGD IAEITRRSVN IFDKTGAEVK RQDIESNLQY DAGDKGIYRH YMQKEIYEQP NAIKNTLTGR ISHGQVDLSE LGPNADELLS KVEHIQILAC GTSYNSGMVS RYWFESLAGI PCDVEIASEF RYRKSAVRRN SLMITLSQSG ETADTLAGLR LSKELGYLGS LAICNVPGSS LVRESDLALM TNAGTEIGVA STKAFTTQLT VLLMLVAKLS RLKGLDASIE HDIVHGLQAL PSRIEQMLSQ DKRIEALAED FSDKHHALFL GRGDQYPIAL EGALKLKEIS YIHAEAYAAG ELKHGPLALI DADMPVIVVA PNNELLEKLK SNIEEVRARG GQLYVFADQD AGFVSSDNMH IIEMPHVEEV IAPIFYTVPL QLLAYHVALI KGTDVDQPRN LAKSVTVE //