FPGS2_ARATH
ID FPGS2_ARATH Reviewed; 625 AA.
AC F4J2K2; A2RVP0; Q8W038; Q9SR80;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Folylpolyglutamate synthase {ECO:0000250|UniProtKB:Q05932, ECO:0000312|EMBL:CAC81075.1};
DE EC=6.3.2.17 {ECO:0000269|PubMed:11752472};
DE AltName: Full=DHFS-FPGS homolog C {ECO:0000312|EMBL:AEE74866.1};
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=FPGS2 {ECO:0000303|PubMed:21070407};
GN Synonyms=ATDFC {ECO:0000312|EMBL:AEE74866.1},
GN DFC {ECO:0000312|EMBL:AEE74866.1}, FPGS3 {ECO:0000312|EMBL:CAC81075.1},
GN FPGSC {ECO:0000303|PubMed:11752472}; OrderedLocusNames=At3g10160;
GN ORFNames=T22K18.1;
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] {ECO:0000305, ECO:0000312|EMBL:CAC81075.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP 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:AEE74866.1}
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:AEE74866.1}
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:AEE74866.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 162-625.
RC STRAIN=cv. Columbia {ECO:0000312|EMBL:ABN04769.1};
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5] {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 [6] {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).
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: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q05932}. Mitochondrion matrix
CC {ECO:0000269|PubMed:11752472}.
CC -!- DISRUPTION PHENOTYPE: Vegetative phenotype does not differ visually
CC from wild-type. No obvious defects in root development.
CC Polyglutamylated folates still detectable, but loss of activity leads
CC to a significant reduction (45%) in total foliar folate abundance
CC compared to wild-type. The reduced total folate content is a result of
CC reduced levels of 5-formyl-THF, 10-formyl and 5,10-methenyl-THF, 5-
CC methyl-THF and THF (42, 42, 53 and 48%, respectively) compared to wild-
CC type. The plastid and mitochondrial folate levels are also reduced by
CC approximately 50 and 55%, respectively compared to wild-type. Folate
CC polyglutamylation levels are significantly reduced but not abolished
CC within the respective compartments. Combined loss of FPGS2 and FPGS1
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 Combined loss of FPGS2 and FPGS3 results in seedling lethality.
CC Seedlings fail to proceed beyond the expanded cotyledon stage, exhibit
CC an albino phenotype and are unable to thrive beyond germination.
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=AAF04408.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ271786; CAC81075.1; -; mRNA.
DR EMBL; AC010927; AAF04408.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74866.1; -; Genomic_DNA.
DR EMBL; BT030031; ABN04769.1; -; mRNA.
DR RefSeq; NP_187627.3; NM_111851.6.
DR AlphaFoldDB; F4J2K2; -.
DR SMR; F4J2K2; -.
DR STRING; 3702.AT3G10160.1; -.
DR iPTMnet; F4J2K2; -.
DR PaxDb; F4J2K2; -.
DR PRIDE; F4J2K2; -.
DR ProteomicsDB; 230110; -.
DR EnsemblPlants; AT3G10160.1; AT3G10160.1; AT3G10160.
DR GeneID; 820179; -.
DR Gramene; AT3G10160.1; AT3G10160.1; AT3G10160.
DR KEGG; ath:AT3G10160; -.
DR Araport; AT3G10160; -.
DR TAIR; locus:2100048; AT3G10160.
DR eggNOG; KOG2525; Eukaryota.
DR HOGENOM; CLU_015869_0_2_1; -.
DR InParanoid; F4J2K2; -.
DR OMA; WERIIHG; -.
DR OrthoDB; 840266at2759; -.
DR BRENDA; 6.3.2.17; 399.
DR UniPathway; UPA00850; -.
DR PRO; PR:F4J2K2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J2K2; baseline and differential.
DR Genevisible; F4J2K2; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:0009853; P:photorespiration; IMP:TAIR.
DR GO; GO:0090351; P:seedling development; IMP:TAIR.
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; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR PANTHER; PTHR11136; PTHR11136; 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 ATP-binding; Ligase; Magnesium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..625
FT /note="Folylpolyglutamate synthase"
FT /id="PRO_0000414486"
FT BINDING 141..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 384
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT CONFLICT 420
FT /note="E -> Q (in Ref. 1; CAC81075)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="G -> D (in Ref. 1; CAC81075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 68921 MW; 3F9CD1CEB0590227 CRC64;
MLVCGKGFLK CRAPGVPFFC DKRKSFFTKT KRGFHSLPLG TGVRVYFNNN LRYSSNSIEV
VEKAAINMGS KEDKADNPAL SSYDDAMEAL STLISRRNRG DRTPTKGNRD KLEQVVTYLK
ILDLEDKIKE LKVIHVAGTK GKGSTCVFSE AILRNCGFRT GMFTSPHLID VRERFRIDGL
DISEEKFLQY FWECWKLLKE KAVDGLTMPP LFQFLTVLAF KIFVCEKVDV AVIEVGLGGK
LDSTNVIQKP VVCGIASLGM DHMDILGNTL ADIAFHKAGI FKPQIPAFTV PQLSEAMDVL
QKTANNLEVP LEVVAPLEPK KLDGVTLGLS GDHQLVNAGL AVSLSRCWLQ RTGNWKKIFP
NESKETEIPV AFCRGLATAR LHGRAQVVHD VVSDPQDSSD SMETPCGDLI FYLDGAHSPE
SMEACGRWFS SAVRGDKSLS TAVNGYMRHG EYGTDLNRVS KQILLFNCME VRDPQVLLPK
LVTTCASSGT HFSRALFVPS MSTYNKVISG ASAIPSDTRR KDLTWQFRLQ RLWEKSIQGT
DAGLDHTLKP DGITALPPHD FLCGDAPQCG GPAGTPVTSS AVMPSLPLTI NWLRDCVRRN
PSLKLEVLVT GSLHLVGDVL RLLKR
