ID   A8F7A8_PSELT            Unreviewed;       598 AA.
AC   A8F7A8;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN   OrderedLocusNames=Tlet_1486 {ECO:0000313|EMBL:ABV34042.1};
OS   Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS   TMO) (Thermotoga lettingae).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Pseudothermotoga.
OX   NCBI_TaxID=416591 {ECO:0000313|EMBL:ABV34042.1, ECO:0000313|Proteomes:UP000002016};
RN   [1] {ECO:0000313|EMBL:ABV34042.1, ECO:0000313|Proteomes:UP000002016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC   {ECO:0000313|Proteomes:UP000002016};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga lettingae TMO.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABV34042.1, ECO:0000313|Proteomes:UP000002016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC   {ECO:0000313|Proteomes:UP000002016};
RX   PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA   Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA   DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA   Noll K.M.;
RT   "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT   the Thermotogales.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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:0000256|ARBA:ARBA00001031};
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DR   EMBL; CP000812; ABV34042.1; -; Genomic_DNA.
DR   RefSeq; WP_012003518.1; NZ_BSDV01000001.1.
DR   AlphaFoldDB; A8F7A8; -.
DR   STRING; 416591.Tlet_1486; -.
DR   MEROPS; C44.A08; -.
DR   KEGG; tle:Tlet_1486; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_012520_7_0_0; -.
DR   OrthoDB; 9779207at2; -.
DR   Proteomes; UP000002016; Chromosome.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
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; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR005855; GFAT.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   NCBIfam; TIGR01135; glmS; 1.
DR   PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR   PANTHER; PTHR10937:SF0; GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); 1.
DR   Pfam; PF13522; GATase_6; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000313|EMBL:ABV34042.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002016};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABV34042.1}.
FT   DOMAIN          2..222
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          285..424
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          449..588
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   598 AA;  67276 MW;  6AAFF16A9D6737F8 CRC64;
     MCGVFGIIFE EEREDLGKIL TAAAKRLVYR GYDSVGIGVV SESGSSDLRK DVGIVDEVNQ
     KLNFEQMKGF KGIVQLRWAT FGTPSQKNAQ PHYDCDKNMI GAHNGNIINT VQLRKLFTEE
     GHTLRSENDG EIVVHAIEKF YDIHHNMDLA IQKAGEILKG DFACVITCVD DRKMYCIKRG
     SSLYLGVGKG FVCASSDLPS IIPLTRRIVP LRDGEYVEFD HCSYRIRDIK TGDEIQREPQ
     IMDISSEAAS KLGFDYYMLK EIYEQPRTTS TLLEFLRFDM DLTRYINILN RARNIFIVGS
     GSSYHASLAG SYFFNKFAKK VSVSCEAGRF VENYANAVGE EDVLILVSQS GETKDVINVL
     NSLDGKCTVL SIVNVTGSTV MMRSLLNVPL CCELEISVPA TKTFINELTV LYYLAAKMSF
     DDNYIKQIKN LPELLEKTLH QAEPQIKELV ESQTNFSDSY VLGYGVMHPV ALEGALKIKE
     VVYRHFEGMY SSEFKHGPLS MVEENYPVFF VTHSSQTNMI VSHINEVTCR NGYAIAISDD
     SEEIASNVMK VVHYPNCPWY LSPFLATIPL QLFAYHFAIR EGKNPDLPRN LSKTVTVD
//