ID V7B1M3_PHAVU Unreviewed; 686 AA.
AC V7B1M3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=PHAVU_008G053200g {ECO:0000313|EMBL:ESW11709.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW11709.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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 ---------------------------------------------------------------------------
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; CM002295; ESW11709.1; -; Genomic_DNA.
DR RefSeq; XP_007139715.1; XM_007139653.1.
DR AlphaFoldDB; V7B1M3; -.
DR STRING; 3885.V7B1M3; -.
DR EnsemblPlants; ESW11709; ESW11709; PHAVU_008G053200g.
DR GeneID; 18621923; -.
DR Gramene; ESW11709; ESW11709; PHAVU_008G053200g.
DR KEGG; pvu:PHAVU_008G053200g; -.
DR eggNOG; KOG1268; Eukaryota.
DR OMA; ASEYRYA; -.
DR OrthoDB; 1705390at2759; -.
DR PhylomeDB; V7B1M3; -.
DR Proteomes; UP000000226; Chromosome 8.
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:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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; 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 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:UP000000226};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..277
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 362..501
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 533..676
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 686 AA; 75506 MW; 3255A3504173FA46 CRC64;
MCGIFAYLNF NVNRERRYIL QVLFNGLRRL EYRGYDSAGI AIDSSSQCAS DAEFPLPHPP
HVFRQEGNIE SLVKSVYQEV GEIKLNLEEP FSTHAGIAHT RWATHGEPAP RNSHPQTSGP
ENEFLVVHNG VITNYEVLKE TLLRHGFTFE SETDTEVIPK LAKFVYDKAN EAADGVTFSQ
VVLEVMRHLE GAYALIFKSP HYPNELIACK RGSPLLLGVK ELTENKGNGS AFEDDKFLSK
DDKPKELFLS SDANAVVEHT KKVLVIEDGE VVHLKDGGAS ILKFDSNMGE NGAFLSRTCS
VRRALSVLEM EVEQINKGHY EHYMQKEIYE QPESLTTTMR GRLIRLGANK SKSVLLGGLK
DHLKTIRRSR RIVFIGCGTS YNAALAARPI LEELSGVPVT MEIASDLLDR EGPIYREDTA
VFVSQSGETA DTLLALEYAL ENGALCVGIT NTVGSAIARN THCGVHINAG AEIGVASTKA
YTSQIVVMVM LSLAIGGDTI SNKARREAII DGLFNLPNKV REVLKLDQEM KDLAKLLIAE
QSLLVFGRGY NYATALEGAL KVKEVALMHS EGILAGEMKH GPLALVDENL PIVVVATRDA
CFSKQQSVIQ QLHARRGRLI VMCSKGDASS VCPNQSCRVI EVPQVEDCLQ PVINVVPLQL
LAYHLTVLRG FNVDQPRNLA KSVTTQ
//