GLMS_THET8
ID GLMS_THET8 Reviewed; 604 AA.
AC Q56213; Q5SH34;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 128.
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};
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=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}; OrderedLocusNames=TTHA1896;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7476196; DOI=10.1111/j.1365-2958.1995.mmi_17010001.x;
RA Fernandez-Herrero L.A., Badet-Denisot M.-A., Badet B., Berenguer J.;
RT "glmS of Thermus thermophilus HB8: an essential gene for cell-wall
RT synthesis identified immediately upstream of the S-layer gene.";
RL Mol. Microbiol. 17:1-12(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
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 -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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DR EMBL; U17352; AAA86988.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71719.1; -; Genomic_DNA.
DR RefSeq; WP_011228994.1; NC_006461.1.
DR RefSeq; YP_145162.1; NC_006461.1.
DR AlphaFoldDB; Q56213; -.
DR SMR; Q56213; -.
DR STRING; 300852.55773278; -.
DR EnsemblBacteria; BAD71719; BAD71719; BAD71719.
DR GeneID; 3168001; -.
DR KEGG; ttj:TTHA1896; -.
DR PATRIC; fig|300852.9.peg.1864; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_0; -.
DR OMA; ASEYRYA; -.
DR PhylomeDB; Q56213; -.
DR Proteomes; UP000000532; 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 3: Inferred from homology;
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..604
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing]"
FT /id="PRO_0000135402"
FT DOMAIN 2..216
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 281..420
FT /note="SIS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 453..594
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 599
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT CONFLICT 53
FT /note="A -> S (in Ref. 1; AAA86988)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="L -> I (in Ref. 1; AAA86988)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="V -> I (in Ref. 1; AAA86988)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="G -> A (in Ref. 1; AAA86988)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="L -> P (in Ref. 1; AAA86988)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="R -> Q (in Ref. 1; AAA86988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 604 AA; 66485 MW; D3D2E400AA4B5A1D CRC64;
MCGIVGYVGF RNATDVLLDG LRRLEYRGYD SAGIAVRTPE GLKVVKRSGK LSALAEAVGK
TPLQGALGIG HTRWATHGAP TDPNAHPHTT EDGRIALIHN GIFENYLELK EALEARGHRF
RSETDTEVLA HLLEETYRGD LLEALREALK AVRGAYAVVV AHEDHEEIVA ARTVSPLVVG
LGEGENFLAS DVPALLPYTR RVLFLHDGDV VRLTREGVEI TDLEGRPVQR EAVEVDWTLE
AAEKGGFPHY MLKEIYEQPW VLENTLGGRL REEEGTVELG LALDPREVDR VHVIACGTAS
YAGLYGKYLL ETLARLPTEW DVASEYRYRD PVVDSRTLAL AISQSGETID TLEGLREAKR
KGARSLGVIN AKGSTLTREV EDVLYIHAGP EIGVASTKAY TAMLAAMALL AVWFGRGRGA
LALEEAQRLL REMRRLPRLV EEVLEKRPLV AHVAEKYHQA RDFLFLGRHV QAPTAYEGAL
KLKEISYIHA EAYPAGEMKH GPIALIDEHL PVVVLATKGP LYEKTLSNIQ EVRARGGKVI
AIATEGDEEI PRLAQDVIYV PEVHPLLAPI VSVVPLQLLA YEIAVLLGRD VDQPRNLAKS
VTVE
