ID   A0A1J0F994_9PHYC        Unreviewed;       595 AA.
AC   A0A1J0F994;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=OS5_039R {ECO:0000313|EMBL:APC25552.1};
OS   Only Syngen Nebraska virus 5.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Algavirales; Phycodnaviridae; Chlorovirus.
OX   NCBI_TaxID=1917232 {ECO:0000313|EMBL:APC25552.1};
RN   [1] {ECO:0000313|EMBL:APC25552.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OSyNE-5 {ECO:0000313|EMBL:APC25552.1};
RX   PubMed=27816636; DOI=10.1016/j.virol.2016.10.013;
RA   Quispe C.F., Esmael A., Sonderman O., McQuinn M., Agarkova I., Battah M.,
RA   Duncan G.A., Dunigan D.D., Smith T.P., De Castro C., Speciale I., Ma F.,
RA   Van Etten J.L.;
RT   "Characterization of a new chlorovirus type with permissive and non-
RT   permissive features on phylogenetically related algal strains.";
RL   Virology 500:103-113(2016).
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; KX857749; APC25552.1; -; Genomic_DNA.
DR   RefSeq; YP_009325557.1; NC_032001.1.
DR   GeneID; 30343853; -.
DR   KEGG; vg:30343853; -.
DR   OrthoDB; 3394at10239; -.
DR   Proteomes; UP000204497; Genome.
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   ECO:0000313|EMBL:APC25552.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000204497};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:APC25552.1}.
FT   DOMAIN          2..227
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          282..421
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          444..585
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   595 AA;  65412 MW;  906EFB675CEEB9E5 CRC64;
     MCGIFGAVSN NNSIEVSIKG IQKLEYRGYD SCGIAYADGD SIERIRSIDG IDDLRKKTLE
     ESSPVAIAHS RWSTTGIPSV VNAHPHISRG TSGCESRIAV VHNGIIENYQ QIRKYLINLG
     YTFDSQTDTE VIAHLIDSQY DGNILHTVQT AVKHLKGSYA IAVMCSKESG KIVVAKQKSP
     LVLGIGSDGA YYIASDVLAL PTNKVVYISD GCSAELSPGG MSIYDSYGNE MEYEVEDVEM
     EQSNLSLDNF DHYMIKEINE QPISILNTIK NKGFYAEIFG EMAHDIFQKI DNILILACGT
     SYHAGLVGKQ WIETIAKIPV NVHIASEYEP TIPRANTLVI TISQSGETAD TIAALQRAQN
     AGMIYTLCIC NSPKSTLVRE SIMKYITRCG SEVSVASTKA FTSQLVVLYI LANVLVNKSD
     DLLNELPEAI ERVIDLTNDE MKHWADEICN AKSAIFLGRG LNAPVAFEGA LKLKEISYIH
     AEGFLGGELK HGPLALLDDK IPVIVTVADH AYLDHIKANI DEVLARNVTV YAIVDQYVNI
     EPQERLHVVK VPFVSKEFSP IIHTIPMQLL SYHVAIKLGK NVDKPRNLAK SVTTF
//