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Folate synthesis bifunctional protein [Includes: 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); Dihydropteroate synthase (DHPS) (EC 2.5.1.15) (Dihydropteroate pyrophosphorylase)]

 FOLKP_CHLPN             Reviewed;         450 AA.
Q9Z7E8;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
28-MAR-2018, entry version 134.
RecName: Full=Folate synthesis bifunctional protein;
Includes:
RecName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase;
Short=HPPK;
EC=2.7.6.3;
AltName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase;
AltName: Full=7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase;
Short=PPPK;
Includes:
RecName: Full=Dihydropteroate synthase;
Short=DHPS;
EC=2.5.1.15;
AltName: Full=Dihydropteroate pyrophosphorylase;
Name=folKP; Synonyms=folP;
OrderedLocusNames=CPn_0758, CP_1114, CpB0786;
Chlamydia pneumoniae (Chlamydophila pneumoniae).
Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
Chlamydia/Chlamydophila group; Chlamydia.
NCBI_TaxID=83558;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CWL029;
PubMed=10192388; DOI=10.1038/7716;
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
"Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
Nat. Genet. 21:385-389(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AR39;
PubMed=10684935; DOI=10.1093/nar/28.6.1397;
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F.,
White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J.,
Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C.,
Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F.,
McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia
pneumoniae AR39.";
Nucleic Acids Res. 28:1397-1406(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=J138;
PubMed=10871362; DOI=10.1093/nar/28.12.2311;
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
"Comparison of whole genome sequences of Chlamydia pneumoniae J138
from Japan and CWL029 from USA.";
Nucleic Acids Res. 28:2311-2314(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=TW-183;
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
"The genome sequence of Chlamydia pneumoniae TW183 and comparison with
other Chlamydia strains based on whole genome sequence analysis.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY: ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP
+ 6-hydroxymethyl-7,8-dihydropterin diphosphate.
-!- CATALYTIC ACTIVITY: 6-hydroxymethyl-7,8-dihydropterin diphosphate
+ 4-aminobenzoate = diphosphate + dihydropteroate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P0AC13};
-!- 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 C-terminal section; belongs to the DHPS family.
{ECO:0000305}.
-!- SIMILARITY: In the N-terminal section; belongs to the HPPK family.
{ECO:0000305}.
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EMBL; AE001363; AAD18896.1; -; Genomic_DNA.
EMBL; AE002161; AAF38881.1; -; Genomic_DNA.
EMBL; BA000008; BAA98966.1; -; Genomic_DNA.
EMBL; AE009440; AAP98715.1; -; Genomic_DNA.
PIR; D86585; D86585.
PIR; G72039; G72039.
RefSeq; NP_224953.1; NC_000922.1.
RefSeq; WP_010883395.1; NZ_LN847257.1.
ProteinModelPortal; Q9Z7E8; -.
SMR; Q9Z7E8; -.
STRING; 182082.CpB0786; -.
EnsemblBacteria; AAD18896; AAD18896; CPn_0758.
EnsemblBacteria; AAF38881; AAF38881; CP_1114.
EnsemblBacteria; AAP98715; AAP98715; CpB0786.
EnsemblBacteria; BAA98966; BAA98966; BAA98966.
GeneID; 894959; -.
KEGG; cpa:CP_1114; -.
KEGG; cpj:folP; -.
KEGG; cpn:CPn0758; -.
KEGG; cpt:CpB0786; -.
PATRIC; fig|115713.3.peg.835; -.
eggNOG; ENOG4105EEI; Bacteria.
eggNOG; COG0294; LUCA.
eggNOG; COG0801; LUCA.
HOGENOM; HOG000063856; -.
KO; K13941; -.
OMA; SLWETEP; -.
OrthoDB; POG091H00BJ; -.
UniPathway; UPA00077; UER00155.
UniPathway; UPA00077; UER00156.
Proteomes; UP000000583; Chromosome.
Proteomes; UP000000801; Chromosome.
GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; PS50972; PTERIN_BINDING; 1.
3: Inferred from homology;
ATP-binding; Complete proteome; Folate biosynthesis; Kinase;
Magnesium; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
Reference proteome; Transferase.
CHAIN 1 450 Folate synthesis bifunctional protein.
/FTId=PRO_0000168240.
DOMAIN 181 440 Pterin-binding. {ECO:0000255|PROSITE-
ProRule:PRU00334}.
REGION 1 166 HPPK.
REGION 183 450 DHPS.
REGION 428 430 6-hydroxymethyl-7,8-dihydropterin
diphosphate binding.
{ECO:0000250|UniProtKB:P0AC13}.
METAL 188 188 Magnesium.
{ECO:0000250|UniProtKB:P9WND1}.
BINDING 228 228 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 268 268 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 288 288 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 358 358 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 394 394 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
SEQUENCE 450 AA; 49815 MW; D644AB80EF4C9A8C CRC64;
MSEPRFVCLS LGSNLGNRFK NLQIARTLLG EQAVLGLRSS VILETEALLL PGSPPEWDLP
YFNSVLVGET TLSLRELLVT IKQIEKVVGR AEESPPWSPR TIDVDILLYG DESFCCDHTE
ITIPLSNLLS RPFLIALIAS LCPYRRFCTQ GSPYHNFTFG ELAHHLPSPP GMIRRSLSPD
TMLMGVVNVT NDSMSDGGMF LDPEKAVAQA EKLFTEGAAV IDFGAQATNP KVKQFLSVDQ
EWERLEPVLR LLKETWSNRK QYPIISLDTF YPEIILRAMD IYPIQWINDV SGGSQSMAEV
ARDCELSLVM NHSSSLPVDP KNILSFSVPI GEQLLSWGEK QLKMFSDVGL NANQVIFDPG
IGFGKGAAQS LATLYEIAKF KRLGCPILIG HSRKSFLSLF GNHDPKDRDW ETVGLSILLQ
QQGVDYLRVH NVAAHQKALS VAACEACAPI


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