ID   A0A077ZWR6_STYLE        Unreviewed;       712 AA.
AC   A0A077ZWR6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, 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   Name=Contig19520.g20691 {ECO:0000313|EMBL:CDW73732.1};
GN   ORFNames=STYLEM_2719 {ECO:0000313|EMBL:CDW73732.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW73732.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW73732.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW73732.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) 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};
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DR   EMBL; CCKQ01002623; CDW73732.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077ZWR6; -.
DR   EnsemblProtists; CDW73732; CDW73732; STYLEM_2719.
DR   InParanoid; A0A077ZWR6; -.
DR   OrthoDB; 1705390at2759; -.
DR   Proteomes; UP000039865; 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; 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; 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; 1.
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   ECO:0000313|EMBL:CDW73732.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDW73732.1}.
FT   DOMAIN          28..302
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          363..520
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          554..700
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   712 AA;  80567 MW;  CE89494954764648 CRC64;
     MLISKLAQRH VKSNPSSLSQ SLAFIATCGF YNYMRKNIEN KNECGGILAY VNKDEDNAQD
     FMMQNAHFLQ KYPYHQCGIA LRDQVSNKVE VRKFTSLGEE QWADQLEHVD HDQFMNKSRI
     SVPQEEDCFF KMSESFTNQD EKIKSRLGVL HSRYASTKGA IKENMAHPHS DEKSRVIVFH
     NGFIANYEDL AKQLYKNQGI KSETDSQLIA KLIGVEMDQG LSVKDAVKSV IEKKLMGTWK
     LAVMSVEQPD HIYFVKNSGN FIIGQSPNSV VVSTQDVVFN EGTVKCETHK IPNNHLVDLK
     DDCTFTMEKL EKKISVERQP KSGFDHIFEE EIYESADAVN AAIDFGKKFI SNHQVYLGGF
     EDQKEELKLI QNLIIAANGS SKLAADYGAH IMKTLQIFNT VRVFDGHDIK KGDLAKVQQG
     GYLTLSQSGE SMHLISALQA ARNQDLTCIN VVNVEDSPIT KVGENLSAQG FDNSQNKNIG
     LYMKAGYCYC DVKSFIPEIV CMALVALWFS DAKTKKQNKE QKKLRQHIIE DLEMLNLRLK
     HALTDPYKNQ YKEVGAFLRD HENLFILAKG TGFMIATYIA EKFTQVTTMH AEAYPSGEFR
     HGPLSMIDEA ERTPVIFIVL NDEHLTQVIS NIGQVRERGA TIVVISLLKD ITKIMDVSRI
     QFLIQLQPTE SMFSALQACT ALQMICYYAS RAKGLNPDQQ VFDAIDFNHE FQ
//