ID A0A0M3ILR2_ASCLU Unreviewed; 230 AA.
AC A0A0M3ILR2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
OS Ascaris lumbricoides (Giant roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0001969001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ALUE_0001969001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 AlphaFoldDB; A0A0M3ILR2; -.
DR WBParaSite; ALUE_0001969001-mRNA-1; ALUE_0001969001-mRNA-1; ALUE_0001969001.
DR Proteomes; UP000036681; Unplaced.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00714; GFAT; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR047084; GFAT_N.
DR InterPro; IPR029055; Ntn_hydrolases_N.
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 SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..230
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 230 AA; 25878 MW; 696C960F33080280 CRC64;
MCGIFAYLNF LTPKKRSEVI DILLRGLQRM EYRGYDSAGI AIDGSNDPAA PHSQIALLKK
VGKVSVLSEY IKENKELDFD AVYNIHCGIA HTRWATHGSP KDVNSHPQRS NKKNEFLVVH
NGIITNYREV KEYLMKKGHE FESETDTEVI AKLIQHIADK YPGFSFRQLV ETAIQQLEGA
FALAFKSSRF PGQLVATRRG SPLLVGIKSS SRLSTDHFPV FFSKGPFIFS
//
