ID   A0A0C2DEC2_9BILA        Unreviewed;       762 AA.
AC   A0A0C2DEC2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=ANCDUO_08959 {ECO:0000313|EMBL:KIH60777.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH60777.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH60777.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH60777.1,
RC   ECO:0000313|Proteomes:UP000054047};
RA   Mitreva M.;
RT   "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KN730640; KIH60777.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2DEC2; -.
DR   Proteomes; UP000054047; Unassembled WGS sequence.
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:1901135; P:carbohydrate derivative metabolic 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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..317
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          426..565
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          597..730
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   762 AA;  84955 MW;  3427FE5D829F685F CRC64;
     MCGIFAYLNF LTPKTRSEII DVLIKGLQRM EYRGYDSAGI AIDGGNEPDS PHKEILLLRK
     AGKVSVLEEA IKESAETLNM DMQYNIHCGI AHTRWATHGS PKDVNSHPQR SNEKNEFMVV
     HNGIITNYRE IKEYLKKKGH KFESETDTEV IAKLIQHIHD RYPDLTFRQL VEIVIQQLEG
     AFALAFKSSK FPGQLVATRR GSPLLIGIKS NNSLQTNHFP VSYSKARRIA SSQATHLRRP
     STAEESFAET PNALDLSSGI RSAHLLDRSR GPVNARPFDS EDWEVEYFVA SDAAAIVEHT
     KQVLFLEDDD VAFVEDGALS IHRITRKFSS ENPQQTREVQ NLNLELQQIM KGNFKTFMQK
     TLQAFGRTDD ESHLPLPCLF SSPSNPLNHV VLGGSEIFEQ PESVVNTMRG RVLPSGQVVL
     GGIKDYIADI KRCRRLIMIA CGTSYHSAIA CRQILEELSE LPVVLELASD FLDRKTPIFR
     DDVCIFISQS GETADTLMAL RYCKPRGALL IGITNTVGSS ICRESHCGVH INAGPEIGVA
     STKAYTSQIL SLLMFALVLS DDRISMMNRR REIINALNQL PNLIREVLEL DKDCLRIAEG
     IYKEKSLLIM GRGFNFATCL EGALKIKELS YLHCEGIMSG ELKHGPLAMV DENLRICMKS
     LNALQQVVAR GGAPFIIADR SVPEKDLAGM KHVLRIPKTV DCVQNILTVI PLQLMAYHIA
     ELNGQNTEDQ QVDRPRNLAK SVTGSLASAN MNMRCSSLDS DK
//