ID A0A0L8GTC7_OCTBM Unreviewed; 677 AA.
AC A0A0L8GTC7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN ORFNames=OCBIM_22028783mg {ECO:0000313|EMBL:KOF79880.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF79880.1};
RN [1] {ECO:0000313|EMBL:KOF79880.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF79880.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF79880.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) 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; KQ420583; KOF79880.1; -; Genomic_DNA.
DR RefSeq; XP_014778461.1; XM_014922975.1.
DR AlphaFoldDB; A0A0L8GTC7; -.
DR EnsemblMetazoa; Ocbimv22028784m; Ocbimv22028784m.p; Ocbimv22028783m.g.
DR EnsemblMetazoa; XM_014922975.1; XP_014778461.1; LOC106875022.
DR GeneID; 106875022; -.
DR OrthoDB; 1705390at2759; -.
DR UniPathway; UPA00113; UER00528.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..284
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 356..495
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 527..668
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 677 AA; 76058 MW; E2C2DD6B1FE848A6 CRC64;
MCGIFAYLNY LTPVTRKQIL NTLITGLKRL EYRGYDSAGV AYEIEGKESE KGSITIIKKP
GKVAALEEEI NSTPVDFDAV STCHIGISHT RWATHGEPNS TNSHPQRSGL NNEFICVHNG
IITNYKDLKS FLESKGFDFE SETDTETIAK LVKHLYDKHK ENKLTFRELI EMTCQQLEGA
YALAFMSTNY PGECVVTRRG SPLLIGIKSN SKLTTDNIPV LYSKDHRGYV EPVQRPTDGT
TEFHPSGPNT EVEYFFASDA SAIIEHTNKV IFLEDDDVAA VTNGCLTIHR IKRNLDDNKV
REVITLKMEI QEIMKGNFSS FMQKEIFEQP ESVVNTMRGR LNFETNQVIL GGIQDFMTEI
RRCRRLLFIA CGTSYHSALA TRQLLEELTE QPVMVELASD FLDRSTPIFR DDVCFFISQS
GETADTLMAL RYCKKRGSLI VGITNTVGSS ICRESNCGVH INAGPEIGVA STKAYTSQFI
ALVMFGLMMC EDRISMQERR KEIIQGLKKL PEDINAVLKL NDEIHSLAQE LYQQKSLLVM
GRGYNFSTCL EGALKIKELT YMHSEGIMAG ELKHGPLALV DKAMPVMMIV TRDKVYSKCM
NALQQVKARH GDLIVICNSG DTETQSQVKK FIAVPHTIDC LQGILTIIPL QLLSLHIAEK
RNCDTDQPRH LLKSYTH
//
