ID A0A2G5V2W5_9PELO Unreviewed; 753 AA.
AC A0A2G5V2W5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=Cnig_chr_II.g5925 {ECO:0000313|EMBL:PIC46132.1};
GN ORFNames=B9Z55_005925 {ECO:0000313|EMBL:PIC46132.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC46132.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIC46132.1}.
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DR EMBL; PDUG01000002; PIC46132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5V2W5; -.
DR STRING; 1611254.A0A2G5V2W5; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000230233; Chromosome ii.
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: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 Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..358
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 430..569
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 601..743
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 753 AA; 84353 MW; 72EB34DD327DEFF1 CRC64;
MCGIFAYLNF LTPKKRSEIV DILVQGLQRM EYRGYDSAGI AIDGSNDIES PHSKVALLRK
AGKVSVLSDF IKESADDLDM DMEYNIHCGI AHTRWATHGS PRDVNSHPHR SNDKNEFLVV
HNGIITNYRE IKEYLEKKGH KFESETDTEV IAKLTQHIHD RYPDFSFRQL VETVIQQLEG
AFALAFKSSR FPGQLVASRR GSPLLVGIKS NSRLQTNHFP VSFSKDAGWK WGDEKQTDGR
RFMSNHATHL RDESSFVETP NNILDLSIDS RDVCNLPVPV DESQRRLSAF MNSLKNAVRS
SNGSAKLEIS DSTTAVRPFD SADWEVEYFV ASDAAAIIEH TKQVLFLEDD DVAFVEDGAL
TIHRISRHAD NGEQKREVQL LEMELQEIMK GSYKTYMQKE IFEQPDSVVN TMRGRLLPSR
QVVLGGIKEY LPDIKRCRRL IMVACGTSFH SAIACRQILE ELSELPVVVE LASDFLDRET
PIFRDDVCLF ISQSGETADT LMALRYCKPR GALTIGVTNT VGSSICRESH CGIHINAGPE
IGVASTKAYT SQILSLLMFA LTLSDDRISM ATRREEIIDA LNDLPNLIRE VLKLDDKVHE
IAQQIYKEKS LLIMGRGFNF ATCLEGALKI KELSYMHCEG IMSGELKHGP LAMVDEFLSI
CMVVCNDHVY KKSLNALQQV VARKGAPIII ADNSVPEGDL AGMKHILRVP KTVDCVQNIL
TVIPLQLLSY HIAELNGANV DRPRNLAKSV TVE
//
