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Folic acid synthesis protein fol1 [Includes: Dihydroneopterin aldolase (DHNA) (EC 4.1.2.25) (7,8-dihydroneopterin aldolase) (FasA) (FasB); 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) (EC 2.7.6.3) (2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase) (7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase) (PPPK) (Dihydropterin pyrophosphokinase) (FasC); Dihydropteroate synthase (DHPS) (EC 2.5.1.15) (Dihydropteroate pyrophosphorylase) (FasD)]

 FOL1_PNECA              Reviewed;         740 AA.
P29251;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
25-OCT-2017, entry version 94.
RecName: Full=Folic acid synthesis protein fol1;
Includes:
RecName: Full=Dihydroneopterin aldolase {ECO:0000303|PubMed:8397083};
Short=DHNA {ECO:0000303|PubMed:7543066};
EC=4.1.2.25 {ECO:0000269|PubMed:7950384, ECO:0000269|PubMed:8397083};
AltName: Full=7,8-dihydroneopterin aldolase;
AltName: Full=FasA {ECO:0000303|PubMed:8397083};
AltName: Full=FasB {ECO:0000303|PubMed:8397083};
Includes:
RecName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000303|PubMed:8397083};
Short=HPPK;
EC=2.7.6.3 {ECO:0000269|PubMed:7950384, ECO:0000269|PubMed:8397083};
AltName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase;
AltName: Full=7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase;
Short=PPPK {ECO:0000303|PubMed:7950384};
AltName: Full=Dihydropterin pyrophosphokinase {ECO:0000303|PubMed:8397083};
AltName: Full=FasC {ECO:0000303|PubMed:8397083};
Includes:
RecName: Full=Dihydropteroate synthase {ECO:0000303|PubMed:8397083};
Short=DHPS {ECO:0000303|PubMed:7950384};
EC=2.5.1.15 {ECO:0000269|PubMed:8397083};
AltName: Full=Dihydropteroate pyrophosphorylase;
AltName: Full=FasD {ECO:0000303|PubMed:8397083};
Name=fol1; Synonyms=fas {ECO:0000303|PubMed:8397083};
Pneumocystis carinii.
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis.
NCBI_TaxID=4754;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1313386; DOI=10.1016/0378-1119(92)90378-3;
Volpes F., Dyer M., Scaife J.G., Darby G., Stammers D.K., Delves C.J.;
"The multifunctional folic acid synthesis fas gene of Pneumocystis
carinii appears to encode dihydropteroate synthase and
hydroxymethyldihydropterin pyrophosphokinase.";
Gene 112:213-218(1992).
[2]
PROTEIN SEQUENCE OF 1-20, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=8397083; DOI=10.1111/j.1432-1033.1993.tb18163.x;
Volpe F., Ballantine S.P., Delves C.J.;
"The multifunctional folic acid synthesis fas gene of Pneumocystis
carinii encodes dihydroneopterin aldolase, hydroxymethyldihydropterin
pyrophosphokinase and dihydropteroate synthase.";
Eur. J. Biochem. 216:449-458(1993).
[3]
PROTEIN SEQUENCE OF 281-293, BIOPHYSICOCHEMICAL PROPERTIES, AND
CATALYTIC ACTIVITY.
PubMed=7950384; DOI=10.1006/prep.1994.1054;
Ballantine S.P., Volpe F., Delves C.J.;
"The hydroxymethyldihydropterin pyrophosphokinase domain of the
multifunctional folic acid synthesis Fas protein of Pneumocystis
carinii expressed as an independent enzyme in Escherichia coli:
refolding and characterization of the recombinant enzyme.";
Protein Expr. Purif. 5:371-378(1994).
[4]
CATALYTIC ACTIVITY.
PubMed=7543066; DOI=10.1016/0378-1119(95)00203-I;
Volpe F., Ballantine S.P., Delves C.J.;
"Two domains with amino-acid sequence similarity are required for
dihydroneopterin aldolase function in the multifunctional folic acid
synthesis Fas protein of Pneumocystis carinii.";
Gene 160:41-46(1995).
[5]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-39; GLY-53;
GLN-63; ASP-161; GLY-175 AND GLN-185.
PubMed=9709001; DOI=10.1021/bi980540x;
Thomas M.C., Ballantine S.P., Bethell S.S., Bains S., Kellam P.,
Delves C.J.;
"Single amino acid substitutions disrupt tetramer formation in the
dihydroneopterin aldolase enzyme of Pneumocystis carinii.";
Biochemistry 37:11629-11636(1998).
-!- FUNCTION: Catalyzes three sequential steps of tetrahydrofolate
biosynthesis. {ECO:0000269|PubMed:8397083}.
-!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-
dihydropterin + glycolaldehyde. {ECO:0000269|PubMed:7543066,
ECO:0000269|PubMed:7950384, ECO:0000269|PubMed:8397083}.
-!- CATALYTIC ACTIVITY: ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP
+ 6-hydroxymethyl-7,8-dihydropterin diphosphate.
{ECO:0000269|PubMed:7543066, ECO:0000269|PubMed:7950384,
ECO:0000269|PubMed:8397083}.
-!- CATALYTIC ACTIVITY: 6-hydroxymethyl-7,8-dihydropterin diphosphate
+ 4-aminobenzoate = diphosphate + dihydropteroate.
{ECO:0000269|PubMed:7543066, ECO:0000269|PubMed:7950384,
ECO:0000269|PubMed:8397083}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P0AC13};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.3 uM for 7,8-dihydroneopterin {ECO:0000269|PubMed:7950384,
ECO:0000269|PubMed:9709001};
KM=3.6 uM for 6-hydroxymethyl-7,8-dihydropterin
{ECO:0000269|PubMed:7950384, ECO:0000269|PubMed:9709001};
Vmax=36 nmol/min/mg enzyme for 7,8-dihydroneopterin
{ECO:0000269|PubMed:7950384, ECO:0000269|PubMed:9709001};
pH dependence:
Optimum pH is 8. {ECO:0000269|PubMed:7950384,
ECO:0000269|PubMed:9709001};
-!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-
amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate
from 7,8-dihydroneopterin triphosphate: step 3/4.
-!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-
amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate
from 7,8-dihydroneopterin triphosphate: step 4/4.
-!- 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.
-!- SIMILARITY: In the N-terminal section; belongs to the DHNA family.
{ECO:0000305}.
-!- SIMILARITY: In the central 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; M86602; AAA33790.1; -; Genomic_DNA.
PIR; S28666; S28666.
ProteinModelPortal; P29251; -.
SMR; P29251; -.
SABIO-RK; P29251; -.
UniPathway; UPA00077; UER00154.
UniPathway; UPA00077; UER00155.
UniPathway; UPA00077; UER00156.
GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-EC.
GO; GO:0102083; F:7,8-dihydromonapterin aldolase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-EC.
GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd00534; DHNA_DHNTPE; 2.
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; IPR006157; FolB_dom.
InterPro; IPR016261; Folic_acid_synth.
InterPro; IPR000550; Hppk.
InterPro; IPR035907; Hppk_sf.
InterPro; IPR000489; Pterin-binding_dom.
Pfam; PF02152; FolB; 2.
Pfam; PF01288; HPPK; 1.
Pfam; PF00809; Pterin_bind; 1.
PIRSF; PIRSF000741; Folic_acid_synth; 1.
SMART; SM00905; FolB; 2.
SUPFAM; SSF51717; SSF51717; 1.
SUPFAM; SSF55083; SSF55083; 1.
TIGRFAMs; TIGR01496; DHPS; 1.
TIGRFAMs; TIGR00526; folB_dom; 2.
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;
Lyase; Magnesium; Metal-binding; Multifunctional enzyme;
Nucleotide-binding; Transferase.
CHAIN 1 740 Folic acid synthesis protein fol1.
/FTId=PRO_0000168242.
DOMAIN 471 730 Pterin-binding. {ECO:0000255|PROSITE-
ProRule:PRU00334}.
REGION 39 160 DHNA 1.
REGION 161 280 DHNA 2.
REGION 291 449 HPPK.
REGION 473 740 DHPS.
REGION 718 720 6-hydroxymethyl-7,8-dihydropterin
diphosphate binding.
{ECO:0000250|UniProtKB:P0AC13}.
METAL 478 478 Magnesium.
{ECO:0000250|UniProtKB:P9WND1}.
BINDING 517 517 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 552 552 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 571 571 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 643 643 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 683 683 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
MUTAGEN 39 39 D->E: Abolishes DHNA activity.
{ECO:0000269|PubMed:9709001}.
MUTAGEN 53 53 G->A: Reduces DHNA activity 11-fold.
{ECO:0000269|PubMed:9709001}.
MUTAGEN 63 63 Q->N: Reduces DHNA activity 16-fold.
{ECO:0000269|PubMed:9709001}.
MUTAGEN 161 161 D->E: No effect.
{ECO:0000269|PubMed:9709001}.
MUTAGEN 175 175 G->A: Abolishes DHNA activity.
{ECO:0000269|PubMed:9709001}.
MUTAGEN 185 185 Q->N: Reduces DHNA activity 24-fold.
{ECO:0000269|PubMed:9709001}.
SEQUENCE 740 AA; 83962 MW; 328F6EB91B4499EB CRC64;
MIFKSLKIFP FYQIYGFRFL KGMIFKKKIH LSKLNKNHDL IHIHSLTLKS IVGKNSWAQR
LLQPVVLTLS MGINASLSGN MDDLSYSIDY ATVYKEVFKL VENSKFENLL DLSDKISKVV
LGDKCKGNWV KVIAETPKGH LLAETGLQII RRKDGIREID DQFFIKNLSL YTIIGINPEE
RVNKQNIIID LILFKSSINL ECKDDFIINT YNIEKLLKEI VKHVEESTFK TIEALALSIA
RISCISHNIE KIIVKVKKSC ALAFAESAGV EIVRSRSCFS SNNYIKSENS IDNEAVYISL
GSNLGNRIKF ILDAIEKMSI KGIKVLKTSM LYESKPMYFK DQPAFYNAVC KVQTSLHPEQ
LLFELQLIEK ELGRVKVIDK GPRCIDLDIV FYGRKIINSE SLIIPHPRVL ERSFVLKPLL
DISGDLVHPV TGLSIASYFE KIVDHDIKPV LPFLYKNKSI DFSFRSYKAP TYIMAILNLT
PDSFFDGGIH SYDSVLIDVE KFINAGATII DIGGQSTRPG SYIIPLEEEI FRVIPAIKYL
QKTYPDILIS IDTFRSEVAE QAVKAGASLV NDISGGRYDP KMFNTVARLK VPICIMHMRG
NFLNMDNLTD YGTDIIEQIT IELEKLLNSA EKSGIPRWNI ILDPGLGFSK TLHQNIELLR
RFNELKSKNC FNGLPWLLGP SRKRFTGFIT GDNMPKDRIW GTVAAVVASI SGGCDIIRVH
DVYEMYKISK MSDAIWKEIY


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