FPGS3_ARATH
ID FPGS3_ARATH Reviewed; 492 AA.
AC Q8W035; F4IWY4; Q8LD20; Q93Y54; Q9M059;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Folylpolyglutamate synthase {ECO:0000250|UniProtKB:Q05932, ECO:0000312|EMBL:CAC82079.1};
DE EC=6.3.2.17 {ECO:0000269|PubMed:11752472};
DE AltName: Full=DHFS-FPGS homolog D {ECO:0000312|EMBL:AEE79412.1};
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, ECO:0000312|EMBL:AAK92804.1};
DE Short=Tetrahydrofolate synthase {ECO:0000250|UniProtKB:Q05932};
GN Name=FPGS3 {ECO:0000303|PubMed:21070407};
GN Synonyms=ATDFD {ECO:0000303|PubMed:11752472, ECO:0000312|EMBL:AEE79411.1},
GN DFD {ECO:0000312|EMBL:AEE79412.1}, FPGS4 {ECO:0000312|EMBL:CAC82079.1},
GN FPGSD {ECO:0000303|PubMed:11752472}; OrderedLocusNames=At3g55630;
GN ORFNames=F1I16_40;
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:CAC82079.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Wassilewskija {ECO:0000269|PubMed:11752472};
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:AEE79412.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AEE79412.1}
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:AAM14145.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia {ECO:0000269|PubMed:14593172};
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AEE79412.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, 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 [7] {ECO:0000305}
RP 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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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. {ECO:0000250|UniProtKB:Q05932,
CC ECO:0000269|PubMed:11752472, ECO:0000269|PubMed:21070407}.
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: Cytoplasm {ECO:0000269|PubMed:11752472}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:11130713, ECO:0000269|PubMed:11752472};
CC IsoId=Q8W035-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11130713, ECO:0000269|PubMed:14593172};
CC IsoId=Q8W035-2; Sequence=VSP_042089;
CC Name=3 {ECO:0000269|PubMed:11130713, ECO:0000269|Ref.5};
CC IsoId=Q8W035-3; Sequence=VSP_042088;
CC -!- DISRUPTION PHENOTYPE: Vegetative phenotype does not differ visually
CC from wild-type. No obvious defects in root development.
CC Polyglutamylated folates still detectable. Has significantly reduced
CC methionine levels compared to wild-type. Combined loss of FPGS3 and
CC FPGS2 results in seedling lethality. Seedlings fail to proceed beyond
CC the expanded cotyledon stage, exhibit an albino phenotype and are
CC unable to thrive beyond germination. Fpgs3 and fpgs1 double mutant
CC exhibits dwarfed leaves, late flowering (approximately 13 days after
CC wild-type), reduced fecundity and delayed senescence. Pollination with
CC fpgs3 and fpgs1 double mutant pollen yields at most one or two seeds
CC per silique compared to the yield of full siliques when wild-type
CC stigmas are pollinated with wild-type pollen. There is a 40% reduction
CC in the total of 5-CH(3)-THF pool in fpgs3 and fpgs1 double mutant leaf
CC tissue. Fpgs3 and fpgs1 double mutants have 70% lower methionine
CC content than wild-type. {ECO:0000269|PubMed:21070407,
CC ECO:0000269|PubMed:21233333}.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000250|UniProtKB:Q05932}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB81588.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ292545; CAC82079.1; -; mRNA.
DR EMBL; AL161667; CAB81588.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79411.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79412.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79413.1; -; Genomic_DNA.
DR EMBL; AY050867; AAK92804.1; -; mRNA.
DR EMBL; AY091206; AAM14145.1; -; mRNA.
DR EMBL; AY086255; AAM64329.1; -; mRNA.
DR PIR; T47702; T47702.
DR RefSeq; NP_567026.3; NM_115421.4. [Q8W035-1]
DR RefSeq; NP_851017.1; NM_180686.2. [Q8W035-3]
DR RefSeq; NP_851018.1; NM_180687.2. [Q8W035-2]
DR AlphaFoldDB; Q8W035; -.
DR SMR; Q8W035; -.
DR STRING; 3702.AT3G55630.3; -.
DR iPTMnet; Q8W035; -.
DR PaxDb; Q8W035; -.
DR PRIDE; Q8W035; -.
DR ProteomicsDB; 230558; -. [Q8W035-1]
DR EnsemblPlants; AT3G55630.1; AT3G55630.1; AT3G55630. [Q8W035-3]
DR EnsemblPlants; AT3G55630.2; AT3G55630.2; AT3G55630. [Q8W035-2]
DR EnsemblPlants; AT3G55630.3; AT3G55630.3; AT3G55630. [Q8W035-1]
DR GeneID; 824729; -.
DR Gramene; AT3G55630.1; AT3G55630.1; AT3G55630. [Q8W035-3]
DR Gramene; AT3G55630.2; AT3G55630.2; AT3G55630. [Q8W035-2]
DR Gramene; AT3G55630.3; AT3G55630.3; AT3G55630. [Q8W035-1]
DR KEGG; ath:AT3G55630; -.
DR Araport; AT3G55630; -.
DR TAIR; locus:2078936; AT3G55630.
DR eggNOG; KOG2525; Eukaryota.
DR HOGENOM; CLU_015869_0_2_1; -.
DR InParanoid; Q8W035; -.
DR PhylomeDB; Q8W035; -.
DR BioCyc; ARA:AT3G55630-MON; -.
DR UniPathway; UPA00850; -.
DR PRO; PR:Q8W035; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8W035; baseline and differential.
DR Genevisible; Q8W035; AT.
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:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046901; P:tetrahydrofolylpolyglutamate biosynthetic process; IBA:GO_Central.
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 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; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..492
FT /note="Folylpolyglutamate synthase"
FT /id="PRO_0000414487"
FT BINDING 68..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 134..155
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11130713, ECO:0000303|Ref.5"
FT /id="VSP_042088"
FT VAR_SEQ 173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11130713,
FT ECO:0000303|PubMed:14593172"
FT /id="VSP_042089"
FT CONFLICT 121
FT /note="C -> S (in Ref. 5; AAM64329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 55167 MW; 59A7436E828366AF CRC64;
MATEDDGELS ARYQNTLDAL SSLITKRGRL ASNNQSHRFR LLFHYLKVLE LEDAVSQMKI
IHVAGTKGKG STCTFAESIL RCYGLRTGLF TSPHLIDVRE RFRLNGIEIS QEKFVNYFWC
CFHKLKEKTS NEVPMPTYFC FLALLAFKIF TTEQVDVVIL EVGLGGRFDA TNVIQKPVVC
GISSLGYDHM EILGYTLAEI AAEKAGIFKS GVPAFTVAQP DEAMRVLNEK ASKLEVNLQV
VEPLDSSQRL GLQGEHQYLN AGLAVALCST FLKEIGIEDK NGLDQTNGLP EKFISGLSNA
YLMGRAMIVP DSELPEEIVY YLDGAHSPES MEACAIWFSK QIKQNQERNQ KRSEQILLFN
CMSVRDPSLL LPRLRSKCID QGVDFKRAVF VPNVSVYNQV GSSTNVGTRV ESMSWQFGLQ
RIWESLARGE AKSNSKSDSK GKEEEKSFVF SSLPVAVDWL RDNARQSKQV RFQVLVTGSL
HLVGDLLRFI KK
