FOLM_PEA
ID FOLM_PEA Reviewed; 515 AA.
AC O04862;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Folate synthesis bifunctional protein, mitochondrial {ECO:0000303|PubMed:9118956};
DE Includes:
DE RecName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000303|PubMed:9118956};
DE Short=HPPK {ECO:0000303|PubMed:9118956};
DE EC=2.7.6.3 {ECO:0000269|PubMed:9118956};
DE AltName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase;
DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase;
DE Short=PPPK;
DE Includes:
DE RecName: Full=Dihydropteroate synthase {ECO:0000303|PubMed:9118956};
DE Short=DHPS {ECO:0000303|PubMed:9118956};
DE EC=2.5.1.15 {ECO:0000269|PubMed:9118956};
DE Flags: Precursor;
GN Name=MitHPPK/DHPS {ECO:0000303|PubMed:9118956};
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888 {ECO:0000312|EMBL:CAA69903.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-40; 121-136; 328-338 AND
RP 415-431, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, SUBCELLULAR LOCATION, SUBUNIT, AND LACK OF INDUCTION BY LIGHT.
RC STRAIN=cv. Douce Provence;
RX PubMed=9118956; DOI=10.1093/emboj/16.5.947;
RA Rebeille F., Macherel D., Mouillon J.M., Garin J., Douce R.;
RT "Folate biosynthesis in higher plants: purification and molecular cloning
RT of a bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8-
RT dihydropteroate synthase localized in mitochondria.";
RL EMBO J. 16:947-957(1997).
CC -!- FUNCTION: Catalyzes the first two consecutive steps of tetrahydrofolate
CC biosynthesis. {ECO:0000269|PubMed:9118956}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-
CC 6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841,
CC ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;
CC Evidence={ECO:0000269|PubMed:9118956};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate =
CC 7,8-dihydropteroate + diphosphate; Xref=Rhea:RHEA:19949,
CC ChEBI:CHEBI:17836, ChEBI:CHEBI:17839, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:72950; EC=2.5.1.15;
CC Evidence={ECO:0000269|PubMed:9118956};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0AC13};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 uM for 6-hydroxymethyl-7,8-dihydropterin
CC {ECO:0000269|PubMed:9118956};
CC KM=70 uM for ATP {ECO:0000269|PubMed:9118956};
CC KM=30 uM for 6-hydroxymethyl-7,8-dihydropterin-pyrophosphate
CC {ECO:0000269|PubMed:9118956};
CC KM=0.6 uM for p-aminobenzoic acid {ECO:0000269|PubMed:9118956};
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:9118956};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:9118956};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 4/4. {ECO:0000305}.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-
CC dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homomultimer. {ECO:0000269|PubMed:9118956}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9118956}.
CC -!- INDUCTION: Not induced by light. {ECO:0000269|PubMed:9118956}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HPPK family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the DHPS family.
CC {ECO:0000305}.
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DR EMBL; Y08611; CAA69903.1; -; mRNA.
DR PIR; T06595; T06595.
DR AlphaFoldDB; O04862; -.
DR SMR; O04862; -.
DR EnsemblPlants; Psat2g131720.1; Psat2g131720.1.cds; Psat2g131720.
DR Gramene; Psat2g131720.1; Psat2g131720.1.cds; Psat2g131720.
DR SABIO-RK; O04862; -.
DR UniPathway; UPA00077; UER00155.
DR UniPathway; UPA00077; UER00156.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IDA:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0046656; P:folic acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00739; DHPS; 1.
DR CDD; cd00483; HPPK; 1.
DR Gene3D; 3.20.20.20; -; 1.
DR Gene3D; 3.30.70.560; -; 1.
DR InterPro; IPR045031; DHP_synth.
DR InterPro; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
DR PANTHER; PTHR20941; PTHR20941; 1.
DR Pfam; PF01288; HPPK; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR SUPFAM; SSF55083; SSF55083; 1.
DR TIGRFAMs; TIGR01496; DHPS; 1.
DR TIGRFAMs; TIGR01498; folK; 1.
DR PROSITE; PS00792; DHPS_1; 1.
DR PROSITE; PS00793; DHPS_2; 1.
DR PROSITE; PS00794; HPPK; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Folate biosynthesis; Kinase;
KW Magnesium; Metal-binding; Mitochondrion; Multifunctional enzyme;
KW Nucleotide-binding; Transferase; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:9118956"
FT CHAIN 29..515
FT /note="Folate synthesis bifunctional protein,
FT mitochondrial"
FT /id="PRO_5000146957"
FT DOMAIN 230..498
FT /note="Pterin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT REGION 47..172
FT /note="HPPK"
FT /evidence="ECO:0000305"
FT REGION 232..515
FT /note="DHPS"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WND1"
FT BINDING 277
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 314
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 333
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 406
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 451
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 486..488
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
SQ SEQUENCE 515 AA; 56455 MW; E6D03CB710CCB56A CRC64;
MSILKCLGVR GNQLCAARNY LKVLGFSSFH TAPNSSIEIQ TQDEEVVIAL GSNVGDRLHN
FKEALKLMRK SGIHITRHAS LYETAPAYVT DQPRFLNSAV RADTKLGPHE LLAALKRIEK
DMGRTDGIRY GPRPIDLDIL FYGKFKVRSD ILTVPHERIW ERPFVMAPLM DLLGTAIDSD
TVASWHSFSG HSGGLNALWE KLGGESLIGE EGMYRVMPVA NGLLDWSRRT LVMGILNLTP
DSFSDGGNFQ SVKSAVSQAR LMISEGADII DIGAQSTRPM ASRISAEEEL GRLIPVLEAV
MSIPEVEGKL ISVDTFYSEV ALEAVRKGAH IINDVSAGKL DASMFKVMAE LDVPYVAMHM
RGDPSTMQDS ENLKYDNVCK DISSELYSRV REAEISGIPA WRIIMDPGIG FSKKTEDNLA
ALTGIPDIRE EISKRSLAIS HAPILIGPSR KRFLGEICSR PSAVDRDPAT IASVTAGVLC
GANIVRVHNV KDNLDAVKLC DAILKQKSSP IKFKQ
