ID   K8EC35_9CHLO            Unreviewed;       780 AA.
AC   K8EC35;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=Bathy03g04790 {ECO:0000313|EMBL:CCO15537.1};
OS   Bathycoccus prasinos.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Bathycoccus.
OX   NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO15537.1, ECO:0000313|Proteomes:UP000198341};
RN   [1] {ECO:0000313|EMBL:CCO15537.1, ECO:0000313|Proteomes:UP000198341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO15537.1,
RC   ECO:0000313|Proteomes:UP000198341};
RA   Genoscope - CEA;
RL   Submitted (OCT-2011) 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; FO082276; CCO15537.1; -; Genomic_DNA.
DR   RefSeq; XP_007514100.1; XM_007514038.1.
DR   AlphaFoldDB; K8EC35; -.
DR   STRING; 41875.K8EC35; -.
DR   GeneID; 19017016; -.
DR   KEGG; bpg:Bathy03g04790; -.
DR   eggNOG; KOG1268; Eukaryota.
DR   OrthoDB; 1705390at2759; -.
DR   Proteomes; UP000198341; Chromosome_3.
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   ECO:0000313|EMBL:CCO15537.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198341};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..357
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          456..596
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          627..770
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   REGION          46..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..60
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   780 AA;  85868 MW;  7854FEA5B78BA803 CRC64;
     MCGIFAYLNC GVPKTKKEIV EKLLVGLKRL EYRGYDSAGF AMDDNEKWCE DDDDDDDDEE
     EGGDKKRHDA KKVIVCREVG KIANLEALAR KELFGEDDDD ENEVKASKSK SSNGRKKSSS
     SIKPLDFCAS IAHTRWATHG PPNKINTHPH TSDSRENEFV VVHNGIITNH APLRAMLERR
     GMKFETDTDT EVIPKLCKFL SDKFEESGEK DVTFRQLAME VTRQLQGAYA LVFKSTKYPG
     ELVAAKRGSP LLMGISDDSG EVSCVIDGNL SDGAEEDVLL KKASGNKKRK SMTGGAAAAA
     AADADTTTTT RITTTTTTTT NNPKVEFYFA SDASAMVEHT KRVLVLEDDD VCHCHDGTYK
     IYKVEKQKHP HPGYTSGHDS PEYGLYKPVV LSKEVERTIE TLEMEVESIM KGEFDHFMQK
     EIFEQPEAIS STMRGRLVLD VLGAAERVML GGMSQFAATI RRSRRIILCG CGTSYNSAIA
     IRQLFEELTE LPVTLELASD VLDRRCPFFR DDTCIFISQS GETADTLKAL EYAKAKGALC
     VGIVNTVGSA ISRATDCGVH INAGAEIGVA STKAYTCQIV AMVLVALSLS EDSRSKHTRR
     DDIMQGLLKL PGCVKECLKM DAILLELAQE LKEEHSLLIF GRGFNYATAL EGALKVKEVA
     LVHSEGILAG EMKHGPLALV DKHMPIIVVC TNDGSYEKQQ SVVQQLKARD GRLILIVSDD
     DTEMEKTAPD AVILRVPKVE DCLQAVVNIV PLQLLSYHLT VLRGHNCDQP RNLAKSVTVE
//