FPGS1_ARATH
ID FPGS1_ARATH Reviewed; 571 AA.
AC F4K2A1; B9DH96; F4K2A2; Q8W040; Q9FI88;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Folylpolyglutamate synthase {ECO:0000250|UniProtKB:Q05932, ECO:0000312|EMBL:CAC80839.2};
DE EC=6.3.2.17 {ECO:0000269|PubMed:11752472};
DE AltName: Full=DHFS-FPGS homolog B {ECO:0000312|EMBL:AED90949.1};
DE AltName: Full=Folylpoly-gamma-glutamate synthetase {ECO:0000250|UniProtKB:Q05932};
DE Short=FPGS {ECO:0000250|UniProtKB:Q05932};
DE AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000250|UniProtKB:Q05932};
DE Short=Tetrahydrofolate synthase {ECO:0000250|UniProtKB:Q05932};
GN Name=FPGS1 {ECO:0000303|PubMed:21070407};
GN Synonyms=ATDFB {ECO:0000303|PubMed:11752472},
GN DFB {ECO:0000312|EMBL:AED90949.1}, FPGS2 {ECO:0000312|EMBL:CAC80839.2},
GN FPGSB {ECO:0000303|PubMed:11752472}; OrderedLocusNames=At5g05980;
GN ORFNames=K18J17.17;
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] {ECO:0000305, ECO:0000312|EMBL:CAC80839.2}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11752472; DOI=10.1073/pnas.261585098;
RA Ravanel S., Cherest H., Jabrin S., Grunwald D., Surdin-Kerjan Y., Douce R.,
RA Rebeille F.;
RT "Tetrahydrofolate biosynthesis in plants: molecular and functional
RT characterization of dihydrofolate synthetase and three isoforms of
RT folylpolyglutamate synthetase in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:15360-15365(2001).
RN [2] {ECO:0000312|EMBL:BAB10803.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000312|EMBL:BAB10803.1};
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [3] {ECO:0000312|EMBL:AED90949.1}
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 [4] {ECO:0000305, ECO:0000312|EMBL:BAH20113.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-571 (ISOFORM 1).
RC STRAIN=cv. Columbia {ECO:0000269|PubMed:19423640};
RC TISSUE=Rosette leaf {ECO:0000312|EMBL:BAH20113.1};
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5] {ECO:0000305}
RP FUNCTION, ALTERNATIVE SPLICING, AND DISRUPTION PHENOTYPE.
RX PubMed=21070407; DOI=10.1111/j.1365-313x.2010.04336.x;
RA Mehrshahi P., Gonzalez-Jorge S., Akhtar T.A., Ward J.L.,
RA Santoyo-Castelazo A., Marcus S.E., Lara-Nunez A., Ravanel S., Hawkins N.D.,
RA Beale M.H., Barrett D.A., Knox J.P., Gregory J.F. III, Hanson A.D.,
RA Bennett M.J., Dellapenna D.;
RT "Functional analysis of folate polyglutamylation and its essential role in
RT plant metabolism and development.";
RL Plant J. 64:267-279(2010).
RN [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21233333; DOI=10.1104/pp.110.168278;
RA Srivastava A.C., Ramos-Parra P.A., Bedair M., Robledo-Hernandez A.L.,
RA Tang Y., Sumner L.W., Diaz de la Garza R.I., Blancaflor E.B.;
RT "The folylpolyglutamate synthetase plastidial isoform is required for
RT postembryonic root development in Arabidopsis.";
RL Plant Physiol. 155:1237-1251(2011).
CC -!- FUNCTION: Catalyzes conversion of folates to polyglutamate derivatives
CC allowing concentration of folate compounds in the cell and the
CC intracellular retention of these cofactors, which are important
CC substrates for most of the folate-dependent enzymes that are involved
CC in one-carbon transfer reactions involved in purine, pyrimidine and
CC amino acid synthesis. Essential for organellar and whole-plant folate
CC homeostasis. Required for postembryonic root development. Generates
CC polyglutamylated folate cofactors to support C1 metabolism required for
CC meristem maintenance and cell expansion during postembryonic root
CC development. {ECO:0000250|UniProtKB:Q05932,
CC ECO:0000269|PubMed:11752472, ECO:0000269|PubMed:21070407,
CC ECO:0000269|PubMed:21233333}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-
CC glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:10580, Rhea:RHEA-COMP:14738,
CC Rhea:RHEA-COMP:14740, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:141005,
CC ChEBI:CHEBI:456216; EC=6.3.2.17;
CC Evidence={ECO:0000269|PubMed:11752472};
CC -!- COFACTOR:
CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC Evidence={ECO:0000250|UniProtKB:Q05932};
CC Note=A monovalent cation. {ECO:0000250|UniProtKB:Q05932};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC biosynthesis. {ECO:0000250|UniProtKB:Q05932}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:11752472}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:11752472, ECO:0000269|PubMed:19423640};
CC IsoId=F4K2A1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4K2A1-2; Sequence=VSP_042087;
CC -!- TISSUE SPECIFICITY: Expressed in both shoots and roots, but expression
CC in roots is higher compared with shoots. Distinct expression in the
CC quiescent center (QC) region of the root tip. Also expressed in
CC vascular tissues of the cotyledons and hypocotyls, and the first true
CC leaves of 7 days old seedlings. {ECO:0000269|PubMed:21233333}.
CC -!- DISRUPTION PHENOTYPE: Has short primary roots. Root hairs are also
CC short and wavy. Epidermal cells of wild-type roots are two times longer
CC than epidermal cells of the mutant roots. Short primary roots of the
CC mutant are impaired in F-actin organization due to extensive bundling.
CC Reduced primary root growth of mutants indicate defects in both cell
CC division and cell expansion. Total folate content does not
CC significantly change between the wild-type and mutant in either shoots
CC or roots. However, differences in the accumulation patterns of some
CC folate classes, and general changes in the contribution of each folate
CC class to the total folate pool are found. A considerable increase in
CC total monoglutamylated folates in mutant roots when compared with wild-
CC type is found. This difference is not observed in shoots. Total
CC polyglutamylated folate content is not altered in either tissue.
CC Nucleotides and amino acids are generally depleted in mutant.
CC Vegetative phenotype does not differ visually from wild-type.
CC Polyglutamylated folates are still detectable in the disruption mutant.
CC In comparison to wild-type, the plastid and mitochondrial folate levels
CC are reduced by approximately 50 and 25%, respectively. Folate
CC polyglutamylation levels are significantly reduced but not abolished
CC within the respective compartments. Combined loss of FPGS1 and FPGS2
CC result in embryo lethality. This double mutant has abnormal seeds that
CC are readily distinguishable as albinos which do not proceed beyond the
CC globular stage of embryogenesis. The absence of a developing embryo
CC lead to collapse of seed walls, leaving shrivelled seed reamnants.
CC FPGS1 and FPGS3 double mutant exhibits dwarfed leaves, late flowering
CC (approximately 13 days after wild-type), reduced fecundity and delayed
CC senescence. Pollination with FPGS1 and FPGS3 double mutant pollen yield
CC at most one or two seeds per silique compared to the yield of full
CC siliques when wild-type stigmas are pollinated with wild-type pollen.
CC There is a 40% reduction in the total of 5-CH(3)-THF pool in FPGS1 and
CC FPGS3 double mutant leaf tissue. FPGS1 and FPGS3 double mutants have
CC 70% lower methionine content than wild-type.
CC {ECO:0000269|PubMed:21070407, ECO:0000269|PubMed:21233333}.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000250|UniProtKB:Q05932}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10803.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ250873; CAC80839.2; -; mRNA.
DR EMBL; AB017060; BAB10803.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90949.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90950.1; -; Genomic_DNA.
DR EMBL; AK317446; BAH20113.1; -; mRNA.
DR RefSeq; NP_001031840.1; NM_001036763.2. [F4K2A1-2]
DR RefSeq; NP_196217.2; NM_120680.3. [F4K2A1-1]
DR AlphaFoldDB; F4K2A1; -.
DR SMR; F4K2A1; -.
DR STRING; 3702.AT5G05980.1; -.
DR PaxDb; F4K2A1; -.
DR PRIDE; F4K2A1; -.
DR ProteomicsDB; 248552; -. [F4K2A1-1]
DR EnsemblPlants; AT5G05980.1; AT5G05980.1; AT5G05980. [F4K2A1-1]
DR EnsemblPlants; AT5G05980.2; AT5G05980.2; AT5G05980. [F4K2A1-2]
DR GeneID; 830484; -.
DR Gramene; AT5G05980.1; AT5G05980.1; AT5G05980. [F4K2A1-1]
DR Gramene; AT5G05980.2; AT5G05980.2; AT5G05980. [F4K2A1-2]
DR KEGG; ath:AT5G05980; -.
DR Araport; AT5G05980; -.
DR TAIR; locus:2153639; AT5G05980.
DR eggNOG; KOG2525; Eukaryota.
DR InParanoid; F4K2A1; -.
DR OrthoDB; 840266at2759; -.
DR BRENDA; 6.3.2.17; 399.
DR UniPathway; UPA00850; -.
DR PRO; PR:F4K2A1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K2A1; baseline and differential.
DR Genevisible; F4K2A1; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IMP:TAIR.
DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0009809; P:lignin biosynthetic process; IMP:TAIR.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:1904961; P:quiescent center organization; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR GO; GO:0010449; P:root meristem growth; IMP:TAIR.
DR GO; GO:0046901; P:tetrahydrofolylpolyglutamate biosynthetic process; IMP:TAIR.
DR Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 1.
DR InterPro; IPR001645; Folylpolyglutamate_synth.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR InterPro; IPR023600; Folylpolyglutamate_synth_euk.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR PANTHER; PTHR11136; PTHR11136; 1.
DR PANTHER; PTHR11136:SF5; PTHR11136:SF5; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR PIRSF; PIRSF038895; FPGS; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR TIGRFAMs; TIGR01499; folC; 1.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chloroplast; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; One-carbon metabolism; Plastid;
KW Reference proteome.
FT CHAIN 1..571
FT /note="Folylpolyglutamate synthase"
FT /id="PRO_0000414485"
FT BINDING 122..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT VAR_SEQ 1..58
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042087"
FT CONFLICT 229
FT /note="Q -> H (in Ref. 1; CAC80839)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 571 AA; 63345 MW; 51192CBC797BBEF4 CRC64;
MFAVSIVPRT TSCRLSSAFL CQLSIPLTLR LHHHYQHHQP HLPSPLSFQI HSLRKQIDMA
AQGGDSYEEA LAALSSLITK RSRADKSNKG DRFELVFDYL KLLDLEEDIL KMNVIHVAGT
KGKGSTCTFT ESIIRNYGFR TGLFTSPHLI DVRERFRLDG VDISEEKFLG YFWWCYNRLK
ERTNEEIPMP TYFRFLALLA FKIFAAEEVD AAILEVGLGG KFDATNAVQK PVVCGISSLG
YDHMEILGDT LGKIAGEKAG IFKLGVPAFT VPQPDEAMRV LEEKASETEV NLEVVQPLTA
RLLSGQKLGL DGEHQYVNAG LAVSLASIWL QQIGKLEVPS RTQMSILPEK FIKGLATASL
QGRAQVVPDQ YTESRTSGDL VFYLDGAHSP ESMEACAKWF SVAVKGDNQS GSSGHLVNGS
AGSSHDKWSN ETCEQILLFN CMSVRDPNLL LPHLKNMCAK YGVNFKKALF VPNMSVYHKV
GTAADLPEND PQVDLSWQFT LQKVWESLVQ SERDGEKDGE SDGNSEVFTS LPMAIKCLRD
TVHESSSATR FQVLVTGSLH LVGDVLRLIR K
