ID   GLMS_SULTO              Reviewed;         589 AA.
AC   F9VPA4;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000255|HAMAP-Rule:MF_00164};
DE            EC=2.6.1.16 {ECO:0000255|HAMAP-Rule:MF_00164, ECO:0000269|PubMed:29507091};
DE   AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=GFAT {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=Glutamine:fructose-6-phosphate amidotransferase {ECO:0000303|PubMed:29507091};
DE   AltName: Full=Hexosephosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
GN   Name=glmS {ECO:0000255|HAMAP-Rule:MF_00164};
GN   OrderedLocusNames=STK_21860 {ECO:0000312|EMBL:BAK54751.1};
GN   ORFNames=ST2186 {ECO:0000303|PubMed:29507091};
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=29507091; DOI=10.1128/jb.00048-18;
RA   Dadashipour M., Iwamoto M., Hossain M.M., Akutsu J.I., Zhang Z.,
RA   Kawarabayasi Y.;
RT   "Identification of a direct biosynthetic pathway for UDP-N-
RT   acetylgalactosamine from glucosamine-6-phosphate in thermophilic
RT   crenarchaeon Sulfolobus tokodaii.";
RL   J. Bacteriol. 200:E00048-E00048(2018).
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC       fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC       {ECO:0000255|HAMAP-Rule:MF_00164, ECO:0000269|PubMed:29507091}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC         phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00164,
CC         ECO:0000269|PubMed:29507091};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00164}.
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DR   EMBL; BA000023; BAK54751.1; -; Genomic_DNA.
DR   RefSeq; WP_052847024.1; NC_003106.2.
DR   AlphaFoldDB; F9VPA4; -.
DR   SMR; F9VPA4; -.
DR   STRING; 273063.STK_21860; -.
DR   EnsemblBacteria; BAK54751; BAK54751; STK_21860.
DR   GeneID; 1460260; -.
DR   KEGG; sto:STK_21860; -.
DR   PATRIC; fig|273063.9.peg.2482; -.
DR   eggNOG; arCOG00057; Archaea.
DR   OMA; ASEYRYA; -.
DR   OrthoDB; 7487at2157; -.
DR   BioCyc; MetaCyc:MON-20591; -.
DR   Proteomes; UP000001015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00164; GlmS; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR01135; glmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   1: Evidence at protein level;
KW   Aminotransferase; Cytoplasm; Glutamine amidotransferase;
KW   Reference proteome; Repeat; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   CHAIN           2..589
FT                   /note="Glutamine--fructose-6-phosphate aminotransferase
FT                   [isomerizing]"
FT                   /id="PRO_0000448049"
FT   DOMAIN          2..221
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   DOMAIN          286..426
FT                   /note="SIS 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   DOMAIN          445..579
FT                   /note="SIS 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   ACT_SITE        2
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   ACT_SITE        584
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   589 AA;  65497 MW;  911A672535639AC9 CRC64;
     MCGIIGIVSL RESKKLAEMT VSALKRLEYR GYDSVGVASI SSNGLEIRKA KGKVEEVVLQ
     KKIEEMEGYV FLGHTRWATH GPPTDYNAHP HTDCNGNIAV VHNGTIKNYK ELREELESLG
     HKFKSETDTE VIPHLIEEFM KRGMDPFQAF KSAIKSLEGS YAVLAVINGE RRIFFAKKDN
     PLIIGLGEGQ NFIASDIPAF LPYTKRILVI RDDELGFITP ETVYLEDKDG NVINIKERIR
     SVDWDIETAS KEGYPHFMIK EIHESPRAVK ETIDSLMSDI DLVEKVIEEI KNAERVIVIG
     AGTSYHAGLY FSIELNRLGI NSLPVIASEY YNVRSKKGDL VFAISQSGET IDVLQGIRMM
     RNSGAKIISL TNVIESAIAR ESDYKIYMRA GPEIGVAATK TFTTQLASIL FILSVLKKEN
     LKKMEKAPDI VRDTISQVEG LTKKIGEELA KKSNIYYLGR GLSLPLAMEG ALKIKEIAYV
     HAEAYPAGES KHGPISLVEK GFPVVIINDG ELTELLQNNL MEMKARGARI YAVSVNKKMK
     DADVEIELQS EIPVLSIAPV IQLIAYYAAV TKGYDPDKPR NLAKTVTVE