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Database: UniProt
Entry: Q76DQ7_9PHYC
LinkDB: Q76DQ7_9PHYC
Original site: Q76DQ7_9PHYC 
ID   Q76DQ7_9PHYC            Unreviewed;       596 AA.
AC   Q76DQ7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 65.
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=k2-gfat {ECO:0000313|EMBL:BAD15299.1};
OS   Chlorella virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Algavirales; Phycodnaviridae; Chlorovirus.
OX   NCBI_TaxID=10507 {ECO:0000313|EMBL:BAD15299.1};
RN   [1] {ECO:0000313|EMBL:BAD15299.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Yamada T., Sugimoto I., Usami S., Fujie M.;
RT   "Introduction and Expression of a CVK2 GFAT gene in Escherichia coli.";
RL   Submitted (APR-2003) 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; AB107976; BAD15299.1; -; Genomic_DNA.
DR   SMR; Q76DQ7; -.
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   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAD15299.1}.
FT   DOMAIN          2..228
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          283..422
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          445..586
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   596 AA;  65518 MW;  92FE8E57859B6121 CRC64;
     MCGIFGAVSN NNSIEVSIKG IQKLEYRGYD SCGIAYADGD GVIERIRSID GIEDLRKKTL
     EESSPVAIAH SRWSTTGIPS VVNAHPHISR GTSGCESRIA VVHNGIIENY QQIRKYLINL
     GYTFDSQTDT EVIAHLIDSQ YNGNILHTVQ MAVKHLKGSY AIAVMCHKES GKIVVAKQKS
     PLVLGIGSDG AYYIASDVLA LPTNKVVYIS DGFSAELSPG SMTIYDPDGN EVEYEVEDVE
     MEQTSMSLDN FDHYMIKEIN EQPISILNTI KNKGFYAEIF GDLAHEIFQK IDNILILACG
     TSYHAGLVGK QWIETIARIP VDVHIASEYE PTIPRANTLV ITISQSGETA DTIAALQRAQ
     NAGMIYTLCI CNSPKSTLVR ESVMKYITKC GSEVSVASTK AFTSQLVVLY MLANVLANKT
     DDLLGDLPQA IERVICLTND EMKRWADEIC TAKSAIFLGR GLNAPVAFEG ALKLKEISYI
     HAEGFLGGEL KHGPLALLDD KIPVIVTVAD HAYLDHIKAN IDEVLARNVT VYAIVDQYVN
     IEPQERLHVV KVPFVSKEFS PIIHTIPMQL LSYYVAIKLG KNVDKPRNLA KSVTTF
//
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