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Folate synthesis bifunctional protein, mitochondrial [Includes: 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) (EC 2.7.6.3) (2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase) (7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase) (PPPK); Dihydropteroate synthase (DHPS) (EC 2.5.1.15)]

 FOLM_PEA                Reviewed;         515 AA.
O04862;
29-APR-2015, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
25-OCT-2017, entry version 79.
RecName: Full=Folate synthesis bifunctional protein, mitochondrial {ECO:0000303|PubMed:9118956};
Includes:
RecName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000303|PubMed:9118956};
Short=HPPK {ECO:0000303|PubMed:9118956};
EC=2.7.6.3 {ECO:0000269|PubMed:9118956};
AltName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase;
AltName: Full=7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase;
Short=PPPK;
Includes:
RecName: Full=Dihydropteroate synthase {ECO:0000303|PubMed:9118956};
Short=DHPS {ECO:0000303|PubMed:9118956};
EC=2.5.1.15 {ECO:0000269|PubMed:9118956};
Flags: Precursor;
Name=MitHPPK/DHPS {ECO:0000303|PubMed:9118956};
Pisum sativum (Garden pea).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Pisum.
NCBI_TaxID=3888 {ECO:0000312|EMBL:CAA69903.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-40; 121-136;
328-338 AND 415-431, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, COFACTOR, SUBCELLULAR LOCATION, SUBUNIT, AND LACK OF
INDUCTION BY LIGHT.
STRAIN=cv. Douce Provence;
PubMed=9118956; DOI=10.1093/emboj/16.5.947;
Rebeille F., Macherel D., Mouillon J.M., Garin J., Douce R.;
"Folate biosynthesis in higher plants: purification and molecular
cloning of a bifunctional 6-hydroxymethyl-7,8-dihydropterin
pyrophosphokinase/7,8-dihydropteroate synthase localized in
mitochondria.";
EMBO J. 16:947-957(1997).
-!- FUNCTION: Catalyzes the first two consecutive steps of
tetrahydrofolate biosynthesis. {ECO:0000269|PubMed:9118956}.
-!- CATALYTIC ACTIVITY: ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP
+ 6-hydroxymethyl-7,8-dihydropterin diphosphate.
{ECO:0000269|PubMed:9118956}.
-!- CATALYTIC ACTIVITY: 6-hydroxymethyl-7,8-dihydropterin diphosphate
+ 4-aminobenzoate = diphosphate + dihydropteroate.
{ECO:0000269|PubMed:9118956}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P0AC13};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.7 uM for 6-hydroxymethyl-7,8-dihydropterin
{ECO:0000269|PubMed:9118956};
KM=70 uM for ATP {ECO:0000269|PubMed:9118956};
KM=30 uM for 6-hydroxymethyl-7,8-dihydropterin-pyrophosphate
{ECO:0000269|PubMed:9118956};
KM=0.6 uM for p-aminobenzoic acid {ECO:0000269|PubMed:9118956};
pH dependence:
Optimum pH is 9. {ECO:0000269|PubMed:9118956};
Temperature dependence:
Optimum temperature is 50 degrees Celsius.
{ECO:0000269|PubMed:9118956};
-!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-
amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate
from 7,8-dihydroneopterin triphosphate: step 4/4. {ECO:0000305}.
-!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
{ECO:0000305}.
-!- SUBUNIT: Homomultimer. {ECO:0000269|PubMed:9118956}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9118956}.
-!- INDUCTION: Not induced by light. {ECO:0000269|PubMed:9118956}.
-!- SIMILARITY: In the N-terminal section; belongs to the HPPK family.
{ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the DHPS family.
{ECO:0000305}.
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EMBL; Y08611; CAA69903.1; -; mRNA.
PIR; T06595; T06595.
ProteinModelPortal; O04862; -.
SMR; O04862; -.
PRIDE; O04862; -.
UniPathway; UPA00077; UER00155.
UniPathway; UPA00077; UER00156.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004156; F:dihydropteroate synthase activity; IDA:UniProtKB.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0046656; P:folic acid biosynthetic process; IDA:UniProtKB.
GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd00739; DHPS; 1.
CDD; cd00483; HPPK; 1.
Gene3D; 3.20.20.20; -; 1.
Gene3D; 3.30.70.560; -; 1.
InterPro; IPR006390; DHP_synth.
InterPro; IPR011005; Dihydropteroate_synth-like.
InterPro; IPR000550; Hppk.
InterPro; IPR035907; Hppk_sf.
InterPro; IPR000489; Pterin-binding_dom.
Pfam; PF01288; HPPK; 1.
Pfam; PF00809; Pterin_bind; 1.
SUPFAM; SSF51717; SSF51717; 1.
SUPFAM; SSF55083; SSF55083; 1.
TIGRFAMs; TIGR01496; DHPS; 1.
TIGRFAMs; TIGR01498; folK; 1.
PROSITE; PS00792; DHPS_1; 1.
PROSITE; PS00793; DHPS_2; 1.
PROSITE; PS00794; HPPK; 1.
PROSITE; PS50972; PTERIN_BINDING; 1.
1: Evidence at protein level;
ATP-binding; Direct protein sequencing; Folate biosynthesis; Kinase;
Magnesium; Metal-binding; Mitochondrion; Multifunctional enzyme;
Nucleotide-binding; Transferase; Transit peptide.
TRANSIT 1 28 Mitochondrion.
{ECO:0000269|PubMed:9118956}.
CHAIN 29 515 Folate synthesis bifunctional protein,
mitochondrial.
/FTId=PRO_5000146957.
DOMAIN 230 498 Pterin-binding. {ECO:0000255|PROSITE-
ProRule:PRU00334}.
REGION 47 172 HPPK. {ECO:0000305}.
REGION 232 515 DHPS.
REGION 486 488 6-hydroxymethyl-7,8-dihydropterin
diphosphate binding.
{ECO:0000250|UniProtKB:P0AC13}.
METAL 237 237 Magnesium.
{ECO:0000250|UniProtKB:P9WND1}.
BINDING 277 277 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 314 314 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 333 333 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 406 406 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 451 451 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
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


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