GFAT1_ARATH
ID GFAT1_ARATH Reviewed; 677 AA.
AC Q9LIP9; A0A178V979;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 {ECO:0000303|PubMed:30775776};
DE Short=AtGFAT {ECO:0000303|PubMed:12000639};
DE Short=AtGFAT1 {ECO:0000303|PubMed:30775776};
DE Short=Glutamine:fructose-6-phosphate amidotransferase 1 {ECO:0000303|PubMed:30775776};
DE EC=2.6.1.16 {ECO:0000250|UniProtKB:P82808};
DE AltName: Full=D-fructose-6-phosphate amidotransferase GFAT1 {ECO:0000305};
DE AltName: Full=Hexosephosphate aminotransferase GFAT1 {ECO:0000305};
GN Name=GFAT1 {ECO:0000303|PubMed:30775776};
GN OrderedLocusNames=At3g24090 {ECO:0000312|Araport:AT3G24090};
GN ORFNames=F14O13.29 {ECO:0000312|EMBL:BAB03027.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY.
RX PubMed=12000639; DOI=10.1046/j.1365-2583.2002.00326.x;
RA Kato N., Dasgupta R., Smartt C.T., Christensen B.M.;
RT "Glucosamine:fructose-6-phosphate aminotransferase: gene characterization,
RT chitin biosynthesis and peritrophic matrix formation in Aedes aegypti.";
RL Insect Mol. Biol. 11:207-216(2002).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION BY TUNICAMYCIN AND DITHIOTHREITOL.
RC STRAIN=cv. Columbia;
RX PubMed=30775776; DOI=10.1093/jxb/erz055;
RA Vu K.V., Jeong C.Y., Nguyen T.T., Dinh T.T.H., Lee H., Hong S.-W.;
RT "Deficiency of AtGFAT1 activity impairs growth, pollen germination and
RT tolerance to tunicamycin in Arabidopsis.";
RL J. Exp. Bot. 70:1775-1787(2019).
CC -!- FUNCTION: Controls the flux of glucose into the hexosamine biosynthetic
CC pathway (HBP) leading to glucosamine (GlcN) content homeostasis
CC (PubMed:30775776). Involved in regulating the availability of
CC precursors for N- and O-linked glycosylation of proteins
CC (PubMed:30775776). Required during pollen maturation and pollen tube
CC formation by triggering polar deposition of pectin and callose in the
CC pollen cell wall (PubMed:30775776). Promotes tolerance to tunicamycin
CC (Tm), an inhibitor of proteins N-glycosylation in endoplasmic reticulum
CC (ER) (PubMed:30775776). {ECO:0000269|PubMed:30775776}.
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:0000250|UniProtKB:P82808};
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:0000250|UniProtKB:P82808}.
CC -!- SUBUNIT: Homotetramer, may also exist as homodimers.
CC {ECO:0000250|UniProtKB:P53704, ECO:0000250|UniProtKB:Q06210}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers specifically in mature
CC anthers, mature pollen grains and pollen tubes (PubMed:30775776).
CC Barely observed in roots, leaves and stems (PubMed:30775776).
CC {ECO:0000269|PubMed:30775776}.
CC -!- DEVELOPMENTAL STAGE: During flower development, first observed in the
CC late tricellular pollen grains. {ECO:0000269|PubMed:30775776}.
CC -!- INDUCTION: Accumulates in response to tunicamycin (Tm, inhibitor of
CC proteins N-glycosylation in endoplasmic reticulum) and dithiothreitol
CC (DTT, reducing agent that blocks disulfide-bond formation of cytosolic
CC and ER proteins). {ECO:0000269|PubMed:30775776}.
CC -!- DISRUPTION PHENOTYPE: Male gametophytic sterility (PubMed:30775776).
CC Impaired growth and pollen germination associated with reduced
CC glucosamine (GlcN) content, and lower tolerance to tunicamycin (Tm)
CC (PubMed:30775776). Mutant plants exhibit also reactive oxygen species
CC (ROS) production, cell death and a decrease in protein N-glycosylation
CC (PubMed:30775776). Abnormal pollen grains due to defects in a polar
CC deposition of pectin and callose in the pollen cell wall
CC (PubMed:30775776). These phenotypes are suppressed by GlcN
CC supplementation (PubMed:30775776). {ECO:0000269|PubMed:30775776}.
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DR EMBL; AP001297; BAB03027.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76855.1; -; Genomic_DNA.
DR RefSeq; NP_189051.3; NM_113314.4.
DR AlphaFoldDB; Q9LIP9; -.
DR SMR; Q9LIP9; -.
DR STRING; 3702.AT3G24090.1; -.
DR PaxDb; Q9LIP9; -.
DR PRIDE; Q9LIP9; -.
DR ProteomicsDB; 175679; -.
DR EnsemblPlants; AT3G24090.1; AT3G24090.1; AT3G24090.
DR GeneID; 821995; -.
DR Gramene; AT3G24090.1; AT3G24090.1; AT3G24090.
DR KEGG; ath:AT3G24090; -.
DR Araport; AT3G24090; -.
DR TAIR; locus:2076146; AT3G24090.
DR eggNOG; KOG1268; Eukaryota.
DR HOGENOM; CLU_012520_5_0_1; -.
DR InParanoid; Q9LIP9; -.
DR OMA; TSYYSGC; -.
DR OrthoDB; 262871at2759; -.
DR PhylomeDB; Q9LIP9; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIP9; baseline and differential.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IMP:UniProtKB.
DR GO; GO:0010208; P:pollen wall assembly; IMP:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:UniProtKB.
DR GO; GO:0072720; P:response to dithiothreitol; IEP:UniProtKB.
DR GO; GO:1904576; P:response to tunicamycin; IMP:UniProtKB.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IMP:UniProtKB.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR005855; GlmS_trans.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01135; glmS; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 2: Evidence at transcript level;
KW Aminotransferase; Carbohydrate metabolism; Glutamine amidotransferase;
KW Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P82808"
FT CHAIN 2..677
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing] 1"
FT /id="PRO_0000453197"
FT DOMAIN 2..269
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 353..492
FT /note="SIS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 524..667
FT /note="SIS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT BINDING 370..371
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 415..417
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 571
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
SQ SEQUENCE 677 AA; 74605 MW; 80999F3CE1551C56 CRC64;
MCGIFAYLNF HANKERRYIL DVLFNGLRRL EYRGYDSAGI AIDNSSPSSS PLVFRQAGNI
ESLVNSVNEE ITNTDLNLDE VFYFHAGIAH TRWATHGEPA PRNSHPQSSG PGDDFLVVHN
GVITNYEVLK ETLVRHGFTF ESDTDTEVIP KLAKFVFDKA NEEGGQTVTF CEVVFEVMRH
LEGAYALIFK SWHYPNELIA CKLGSPLLLG VKELDQGESN SHVFQDAHFL SKNDHPKEFF
LSSDPHALVE HTKKVLVIED GEVVNLKDGG VSILKFENER GRCNGLSRPA SVERALSVLE
MEVEQISKGK YDHYMQKEIH EQPESLTTTM RGRLIRGGSR KTKTVLLGGL KDHLKTIRRS
RRIVFIGCGT SYNAALASRP ILEELSGIPV SMEIASDLWD RQGPIYREDT AVFVSQSGET
ADTLLALDYA RENGALCVGI TNTVGSSIAR KTHCGVHINA GAEIGVASTK AYTSQIVVMV
MLALAIGSDT ISSQKRREAI IDGLLDLPYK VKEVLKLDDE MKDLAQLLID EQSLLVFGRG
YNYATALEGA LKVKEVALMH SEGILAGEMK HGPLALVDEN LPIAVIATRD ACFSKQQSVI
QQLHARKGRL IVMCSKGDAA SVSSSGSCRA IEVPQVEDCL QPVINIVPLQ LLAYHLTVLR
GHNVDQPRNL AKSVTTQ
