ID B3T893_9ARCH Unreviewed; 584 AA.
AC B3T893;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN ORFNames=ALOHA_HF4000APKG5C13ctg1g8 {ECO:0000313|EMBL:ABZ08802.1};
OS uncultured marine crenarchaeote HF4000_APKG5C13.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC environmental samples.
OX NCBI_TaxID=455591 {ECO:0000313|EMBL:ABZ08802.1};
RN [1] {ECO:0000313|EMBL:ABZ08802.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18580971; DOI=10.1038/ismej.2008.62;
RA Konstantinidis K.T., Delong E.F.;
RT "Genomic patterns of recombination, clonal divergence and environment in
RT marine microbial populations.";
RL ISME J. 2:1052-1065(2008).
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; EU016637; ABZ08802.1; -; Genomic_DNA.
DR AlphaFoldDB; B3T893; -.
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; cd00714; GFAT; 1.
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; IPR047084; GFAT_N.
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:ABZ08802.1}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABZ08802.1}.
FT DOMAIN 2..217
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 275..414
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 437..574
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 584 AA; 64135 MW; 237B3B7893E190BA CRC64;
MCSIIGYRGK NSAAPILVKG LQRMEYRGYD SVGIATKSKN QILLRKGVGK VVEVNNAIQL
DKLPGNIGIG HTRWATHGKV TEQNAHPHSS NSGKIAIVHN GIIENFEELK SNLQKKGFDF
HSETDTEVIA NLIQLNFDEA PDVKQAIIKT VAQLKGHYSF VVIFEDGTIV GARFHEPLIV
GVGKNSYYLS SDVLGFIEKT DDAIYLDNED FVILNDAGIH IFGFDGSSVK YQITKVSKEF
ADVYKGDYAH FTIKEISEQP DSILRAGNND QIQQFVDGIK QAKNLYITGS GTSYNAAEIA
KYLMSKFAKI KINTVIASEL AFSPDDIEQN STLVAISQSG ESADVLEAVK IAKKSNAIIL
SVVNHLNSSL SQESSLVIGL NCGPEIGVAA TKSFTSQLTI LYKITDKLCN GCINPDWEKV
STIISQILSN HSKIKEIAKD LKEVSDIYVL GRGIHLPIAR EAALKLKELS YIHAEGIAGG
ELKHGPLALM DSNVYVIIIN PNDSTYNDTL NTAHEIKARG AKIIGISDKE SDVYDYWVEI
PTIDESLYPI IEIIPIQLLA YYSALEKKTN PDYPRNLAKS VTVK
//