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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//