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Folylpolyglutamate synthase (EC 6.3.2.17) (DHFS-FPGS homolog B) (Folylpoly-gamma-glutamate synthetase) (FPGS) (Tetrahydrofolylpolyglutamate synthase) (Tetrahydrofolate synthase)

 FPGS1_ARATH             Reviewed;         571 AA.
F4K2A1; B9DH96; F4K2A2; Q8W040; Q9FI88;
14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
23-MAY-2018, entry version 59.
RecName: Full=Folylpolyglutamate synthase {ECO:0000250|UniProtKB:Q05932, ECO:0000312|EMBL:CAC80839.2};
EC=6.3.2.17 {ECO:0000269|PubMed:11752472};
AltName: Full=DHFS-FPGS homolog B {ECO:0000312|EMBL:AED90949.1};
AltName: Full=Folylpoly-gamma-glutamate synthetase {ECO:0000250|UniProtKB:Q05932};
Short=FPGS {ECO:0000250|UniProtKB:Q05932};
AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000250|UniProtKB:Q05932};
Short=Tetrahydrofolate synthase {ECO:0000250|UniProtKB:Q05932};
Name=FPGS1 {ECO:0000303|PubMed:21070407};
Synonyms=ATDFB {ECO:0000303|PubMed:11752472},
DFB {ECO:0000312|EMBL:AED90949.1},
FPGS2 {ECO:0000312|EMBL:CAC80839.2},
FPGSB {ECO:0000303|PubMed:11752472}; OrderedLocusNames=At5g05980;
ORFNames=K18J17.17;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1] {ECO:0000305, ECO:0000312|EMBL:CAC80839.2}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
SUBSTRATE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=11752472; DOI=10.1073/pnas.261585098;
Ravanel S., Cherest H., Jabrin S., Grunwald D., Surdin-Kerjan Y.,
Douce R., Rebeille F.;
"Tetrahydrofolate biosynthesis in plants: molecular and functional
characterization of dihydrofolate synthetase and three isoforms of
folylpolyglutamate synthetase in Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 98:15360-15365(2001).
[2] {ECO:0000312|EMBL:BAB10803.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia {ECO:0000312|EMBL:BAB10803.1};
PubMed=10470850; DOI=10.1093/dnares/6.3.183;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IX.
Sequence features of the regions of 1,011,550 bp covered by seventeen
P1 and TAC clones.";
DNA Res. 6:183-195(1999).
[3] {ECO:0000312|EMBL:AED90949.1}
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4] {ECO:0000305, ECO:0000312|EMBL:BAH20113.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-571 (ISOFORM 1).
STRAIN=cv. Columbia {ECO:0000269|PubMed:19423640};
TISSUE=Rosette leaf {ECO:0000312|EMBL:BAH20113.1};
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[5] {ECO:0000305}
FUNCTION, ALTERNATIVE SPLICING, AND DISRUPTION PHENOTYPE.
PubMed=21070407; DOI=10.1111/j.1365-313X.2010.04336.x;
Mehrshahi P., Gonzalez-Jorge S., Akhtar T.A., Ward J.L.,
Santoyo-Castelazo A., Marcus S.E., Lara-Nunez A., Ravanel S.,
Hawkins N.D., Beale M.H., Barrett D.A., Knox J.P., Gregory J.F. III,
Hanson A.D., Bennett M.J., Dellapenna D.;
"Functional analysis of folate polyglutamylation and its essential
role in plant metabolism and development.";
Plant J. 64:267-279(2010).
[6] {ECO:0000305}
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=21233333; DOI=10.1104/pp.110.168278;
Srivastava A.C., Ramos-Parra P.A., Bedair M., Robledo-Hernandez A.L.,
Tang Y., Sumner L.W., Diaz de la Garza R.I., Blancaflor E.B.;
"The folylpolyglutamate synthetase plastidial isoform is required for
postembryonic root development in Arabidopsis.";
Plant Physiol. 155:1237-1251(2011).
-!- FUNCTION: Catalyzes conversion of folates to polyglutamate
derivatives allowing concentration of folate compounds in the cell
and the intracellular retention of these cofactors, which are
important substrates for most of the folate-dependent enzymes that
are involved in one-carbon transfer reactions involved in purine,
pyrimidine and amino acid synthesis. Essential for organellar and
whole-plant folate homeostasis. Required for postembryonic root
development. Generates polyglutamylated folate cofactors to
support C1 metabolism required for meristem maintenance and cell
expansion during postembryonic root development.
{ECO:0000250|UniProtKB:Q05932, ECO:0000269|PubMed:11752472,
ECO:0000269|PubMed:21070407, ECO:0000269|PubMed:21233333}.
-!- CATALYTIC ACTIVITY: ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-
glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).
{ECO:0000269|PubMed:11752472}.
-!- COFACTOR:
Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
Evidence={ECO:0000250|UniProtKB:Q05932};
Note=A monovalent cation. {ECO:0000250|UniProtKB:Q05932};
-!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
biosynthesis. {ECO:0000250|UniProtKB:Q05932}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:11752472}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:11752472, ECO:0000269|PubMed:19423640};
IsoId=F4K2A1-1; Sequence=Displayed;
Name=2;
IsoId=F4K2A1-2; Sequence=VSP_042087;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in both shoots and roots, but
expression in roots is higher compared with shoots. Distinct
expression in the quiescent center (QC) region of the root tip.
Also expressed in vascular tissues of the cotyledons and
hypocotyls, and the first true leaves of 7 days old seedlings.
{ECO:0000269|PubMed:21233333}.
-!- DISRUPTION PHENOTYPE: Has short primary roots. Root hairs are also
short and wavy. Epidermal cells of wild-type roots are two times
longer than epidermal cells of the mutant roots. Short primary
roots of the mutant are impaired in F-actin organization due to
extensive bundling. Reduced primary root growth of mutants
indicate defects in both cell division and cell expansion. Total
folate content does not significantly change between the wild-type
and mutant in either shoots or roots. However, differences in the
accumulation patterns of some folate classes, and general changes
in the contribution of each folate class to the total folate pool
are found. A considerable increase in total monoglutamylated
folates in mutant roots when compared with wild-type is found.
This difference is not observed in shoots. Total polyglutamylated
folate content is not altered in either tissue. Nucleotides and
amino acids are generally depleted in mutant. Vegetative phenotype
does not differ visually from wild-type. Polyglutamylated folates
are still detectable in the disruption mutant. In comparison to
wild-type, the plastid and mitochondrial folate levels are reduced
by approximately 50 and 25%, respectively. Folate
polyglutamylation levels are significantly reduced but not
abolished within the respective compartments. Combined loss of
FPGS1 and FPGS2 result in embryo lethality. This double mutant has
abnormal seeds that are readily distinguishable as albinos which
do not proceed beyond the globular stage of embryogenesis. The
absence of a developing embryo lead to collapse of seed walls,
leaving shrivelled seed reamnants. FPGS1 and FPGS3 double mutant
exhibits dwarfed leaves, late flowering (approximately 13 days
after wild-type), reduced fecundity and delayed senescence.
Pollination with FPGS1 and FPGS3 double mutant pollen yield at
most one or two seeds per silique compared to the yield of full
siliques when wild-type stigmas are pollinated with wild-type
pollen. There is a 40% reduction in the total of 5-CH(3)-THF pool
in FPGS1 and FPGS3 double mutant leaf tissue. FPGS1 and FPGS3
double mutants have 70% lower methionine content than wild-type.
{ECO:0000269|PubMed:21070407, ECO:0000269|PubMed:21233333}.
-!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
{ECO:0000250|UniProtKB:Q05932}.
-!- SEQUENCE CAUTION:
Sequence=BAB10803.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ250873; CAC80839.2; -; mRNA.
EMBL; AB017060; BAB10803.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED90949.1; -; Genomic_DNA.
EMBL; CP002688; AED90950.1; -; Genomic_DNA.
EMBL; AK317446; BAH20113.1; -; mRNA.
RefSeq; NP_001031840.1; NM_001036763.2. [F4K2A1-2]
RefSeq; NP_196217.2; NM_120680.3. [F4K2A1-1]
UniGene; At.32924; -.
UniGene; At.66718; -.
ProteinModelPortal; F4K2A1; -.
SMR; F4K2A1; -.
STRING; 3702.AT5G05980.1; -.
PaxDb; F4K2A1; -.
PRIDE; F4K2A1; -.
EnsemblPlants; AT5G05980.1; AT5G05980.1; AT5G05980. [F4K2A1-1]
EnsemblPlants; AT5G05980.2; AT5G05980.2; AT5G05980. [F4K2A1-2]
GeneID; 830484; -.
Gramene; AT5G05980.1; AT5G05980.1; AT5G05980. [F4K2A1-1]
Gramene; AT5G05980.2; AT5G05980.2; AT5G05980. [F4K2A1-2]
KEGG; ath:AT5G05980; -.
Araport; AT5G05980; -.
TAIR; locus:2153639; AT5G05980.
eggNOG; KOG2525; Eukaryota.
eggNOG; COG0285; LUCA.
HOGENOM; HOG000181278; -.
InParanoid; F4K2A1; -.
KO; K01930; -.
OMA; FRSEAYA; -.
OrthoDB; EOG093606Q9; -.
BRENDA; 6.3.2.17; 399.
Reactome; R-ATH-196757; Metabolism of folate and pterines.
UniPathway; UPA00850; -.
PRO; PR:F4K2A1; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; F4K2A1; baseline and differential.
Genevisible; F4K2A1; AT.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IMP:TAIR.
GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
GO; GO:1904961; P:quiescent center organization; IMP:TAIR.
GO; GO:0048364; P:root development; IMP:TAIR.
GO; GO:0048767; P:root hair elongation; IMP:TAIR.
GO; GO:0010449; P:root meristem growth; IMP:TAIR.
GO; GO:0046901; P:tetrahydrofolylpolyglutamate biosynthetic process; IMP:TAIR.
Gene3D; 3.40.1190.10; -; 1.
Gene3D; 3.90.190.20; -; 1.
InterPro; IPR001645; Folylpolyglutamate_synth.
InterPro; IPR018109; Folylpolyglutamate_synth_CS.
InterPro; IPR023600; Folylpolyglutamate_synth_euk.
InterPro; IPR036565; Mur-like_cat_sf.
InterPro; IPR036615; Mur_ligase_C_dom_sf.
InterPro; IPR013221; Mur_ligase_cen.
PANTHER; PTHR11136; PTHR11136; 1.
Pfam; PF08245; Mur_ligase_M; 1.
PIRSF; PIRSF038895; FPGS; 1.
SUPFAM; SSF53244; SSF53244; 2.
SUPFAM; SSF53623; SSF53623; 1.
TIGRFAMs; TIGR01499; folC; 1.
PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Chloroplast; Complete proteome;
Ligase; Magnesium; Metal-binding; Nucleotide-binding;
One-carbon metabolism; Plastid; Reference proteome.
CHAIN 1 571 Folylpolyglutamate synthase.
/FTId=PRO_0000414485.
NP_BIND 122 125 ATP. {ECO:0000250|UniProtKB:P08192}.
METAL 146 146 Magnesium 1.
{ECO:0000250|UniProtKB:P08192}.
METAL 215 215 Magnesium 1.
{ECO:0000250|UniProtKB:P08192}.
METAL 243 243 Magnesium 2.
{ECO:0000250|UniProtKB:P08192}.
BINDING 363 363 ATP. {ECO:0000250|UniProtKB:P08192}.
BINDING 385 385 ATP. {ECO:0000250|UniProtKB:P08192}.
VAR_SEQ 1 58 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_042087.
CONFLICT 229 229 Q -> H (in Ref. 1; CAC80839).
{ECO:0000305}.
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


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