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Database: UniProt
Entry: V7B1M3_PHAVU
LinkDB: V7B1M3_PHAVU
Original site: V7B1M3_PHAVU 
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};
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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
//
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