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Database: UniProt
Entry: A0A091GN53_9AVES
LinkDB: A0A091GN53_9AVES
Original site: A0A091GN53_9AVES 
ID   A0A091GN53_9AVES        Unreviewed;       680 AA.
AC   A0A091GN53;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   13-SEP-2023, entry version 23.
DE   RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
DE   Flags: Fragment;
GN   ORFNames=N303_12519 {ECO:0000313|EMBL:KFO82629.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO82629.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO82629.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO82629.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-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};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC       glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-
CC       fructose 6-phosphate: step 1/1. {ECO:0000256|ARBA:ARBA00004775}.
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DR   EMBL; KL448314; KFO82629.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091GN53; -.
DR   STRING; 55661.A0A091GN53; -.
DR   UniPathway; UPA00113; UER00528.
DR   Proteomes; UP000053760; 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:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
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:SF12; GLUTAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE [ISOMERIZING] 1; 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:0000313|EMBL:KFO82629.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFO82629.1}.
FT   DOMAIN          1..286
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          358..497
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          529..670
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO82629.1"
FT   NON_TER         680
FT                   /evidence="ECO:0000313|EMBL:KFO82629.1"
SQ   SEQUENCE   680 AA;  76586 MW;  24DCB9A06360713B CRC64;
     TGIFAYLNYH VPRTRREILE TLIKGLQRLE YRGYDSAGVG IDGGNDKDWE ANACKIQLIK
     QKGKVKALDE EVHKQQDIDL DIEFDVHLGI AHTRWATHGE PNPVNSHPQR SDKNNEFIVI
     HNGIITNYKD LRKFLESKGY DFESETDTES IAKLVKYMYD NRDSDDISFT TLVERVIQQL
     EGAFALVFKS IHYPGQAVGT RRGSPLLIGV RSEHKLSTDH IPILYRTGKD KKGSCSLSRV
     DSTTCLFPVE EKAVEYYFAS DASAVIEHTN RVIFLEDDDV AAVVDGRLSI HRIKRTAGDH
     PGRAVQTLQM ELQQIMKGNF SSFMQKEIFE QPESVVNTMR GRVNFDDYTV NLGGLKDHIK
     EIQRCRRLIL IACGTSYHAG VATRQVLEEL TELPVMVELA SDFLDRNTPV FRDDVCFFIS
     QSGETADTLM GLRYCKERGA LTVGITNTVG SSISRETDCG VHINAGPEIG VASTKAYTSQ
     FVSLVMFALM MCDDRISMQE RRKEIMRGLK GLPDLIKEVL SMDDEIQKLA TELYHQKSVL
     IMGRGYHYAT CLEGALKIKE ITYMHSEGIL AGELKHGPLA LVDKLMPVIM IIMRDHTYAK
     CQNALQQVIA RQGRPVVICD KEDIETIKNN KRTIKVPHSV DCLQGILSVI PLQLLAFHLA
     VLRGYDVDFP RNLAKSVTVE
//
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