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Database: UniProt
Entry: I3K5G4_ORENI
LinkDB: I3K5G4_ORENI
Original site: I3K5G4_ORENI 
ID   I3K5G4_ORENI            Unreviewed;       685 AA.
AC   I3K5G4;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 55.
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=LOC100692652 {ECO:0000313|Ensembl:ENSONIP00000016359.2};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000016359.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000016359.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_019222572.1; XM_019367027.1.
DR   AlphaFoldDB; I3K5G4; -.
DR   STRING; 8128.ENSONIP00000081467; -.
DR   Ensembl; ENSONIT00000016374.2; ENSONIP00000016359.2; ENSONIG00000013006.2.
DR   GeneID; 100692652; -.
DR   KEGG; onl:100692652; -.
DR   CTD; 9945; -.
DR   eggNOG; KOG1268; Eukaryota.
DR   GeneTree; ENSGT00940000156413; -.
DR   HOGENOM; CLU_012520_5_2_1; -.
DR   OrthoDB; 1705390at2759; -.
DR   TreeFam; TF300864; -.
DR   UniPathway; UPA00113; UER00528.
DR   Proteomes; UP000005207; Linkage group LG2.
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:SF10; GLUTAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE [ISOMERIZING] 2; 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   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..291
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          363..502
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          534..675
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   REGION          230..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   685 AA;  77202 MW;  E7DC2EBEB9D647AE CRC64;
     MCGIFAYLNY RVPRTRKEIF ETLVKGLQRL EYRGYDSAGI AVDGPSKTTS DQNNNSICLI
     KKTGKVKALD EELYKKDSLN LDEELCTHFG IAHTRWATHG EPSALNSHPQ RSDKDNEFVV
     IHNGIITNYK ELKKYLINKG YEFESETDTE VIPKLIKYIY DNRENDSITF SKLVERVIKQ
     LEGAFALVFK SRHFPGEAVA TRRGSPMVIG VRSEHELLTE HIPVQYNSAH HKEEVHEKNT
     RNRADSSSNI NSVGDGRAVE FYFASDASAI IEHTNKVLYM EDDDIAVVTG GKLSIHRMNR
     QAGEDPVRAI MTLQMELQQI MKGNFDAFMQ KEIFEQPESV VNTMRGRICF DTKKVVLGGL
     KDHLKEIKRC RRLIMIGCGT SFHAAVATRQ ILEELTELPV MVELASDFLD RITPVFRDDV
     CFFISQSGET ADTLMALRYC KDRGALTVGV TNTVGSSICR ETDCGVHINA GPEIGVASTK
     AYTSQFVSLI MFGLMMSEDR LSLQKRREEI INSLKMLPEL IKKVLSLDEK IKAIANELYQ
     QRSLLVMGRG FNYATCLEGA LKIKEITYMH SEGILAGELK HGPLALVDKH MPVIMIIMRD
     ACYTKCQNAL QQVTARSGRP IIICCQDDTE LTKNAYQTIE LPQTVDCLQG ILSVIPLQLM
     SFHLAVLRGY DVDFPRNLAK SVTVE
//
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