ID   FOLKP_CHLTR             Reviewed;         450 AA.
AC   O84619;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Folate synthesis bifunctional protein;
DE   Includes:
DE     RecName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase;
DE              Short=HPPK;
DE              EC=2.7.6.3;
DE     AltName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase;
DE     AltName: Full=7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase;
DE              Short=PPPK;
DE   Includes:
DE     RecName: Full=Dihydropteroate synthase;
DE              Short=DHPS;
DE              EC=2.5.1.15;
DE     AltName: Full=Dihydropteroate pyrophosphorylase;
GN   Name=folKP; OrderedLocusNames=CT_613;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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   -!- 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0AC13};
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.
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   -!- SIMILARITY: In the C-terminal section; belongs to the DHPS family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the HPPK family.
CC       {ECO:0000305}.
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DR   EMBL; AE001273; AAC68216.1; -; Genomic_DNA.
DR   PIR; A71494; A71494.
DR   RefSeq; NP_220130.1; NC_000117.1.
DR   RefSeq; WP_009871981.1; NC_000117.1.
DR   AlphaFoldDB; O84619; -.
DR   SMR; O84619; -.
DR   STRING; 272561.CT_613; -.
DR   EnsemblBacteria; AAC68216; AAC68216; CT_613.
DR   GeneID; 884393; -.
DR   KEGG; ctr:CT_613; -.
DR   PATRIC; fig|272561.5.peg.670; -.
DR   HOGENOM; CLU_008023_2_2_0; -.
DR   InParanoid; O84619; -.
DR   OrthoDB; 9811744at2; -.
DR   BioCyc; MetaCyc:MONOMER-18794; -.
DR   UniPathway; UPA00077; UER00155.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004156; F:dihydropteroate synthase activity; IBA:GO_Central.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IBA:GO_Central.
DR   CDD; cd00739; DHPS; 1.
DR   CDD; cd00483; HPPK; 1.
DR   Gene3D; 3.30.70.560; 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK; 1.
DR   Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR   InterPro; IPR045031; DHP_synth-like.
DR   InterPro; IPR006390; DHP_synth_dom.
DR   InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR   InterPro; IPR000550; Hppk.
DR   InterPro; IPR035907; Hppk_sf.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   NCBIfam; TIGR01496; DHPS; 1.
DR   NCBIfam; TIGR01498; folK; 1.
DR   PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1.
DR   PANTHER; PTHR20941:SF1; FOLIC ACID SYNTHESIS PROTEIN FOL1; 1.
DR   Pfam; PF01288; HPPK; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   SUPFAM; SSF55083; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK; 1.
DR   SUPFAM; SSF51717; Dihydropteroate synthetase-like; 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   3: Inferred from homology;
KW   ATP-binding; Folate biosynthesis; Kinase; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..450
FT                   /note="Folate synthesis bifunctional protein"
FT                   /id="PRO_0000168241"
FT   DOMAIN          180..441
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT   REGION          1..166
FT                   /note="HPPK"
FT   REGION          182..450
FT                   /note="DHPS"
FT   BINDING         187
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WND1"
FT   BINDING         227
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         267
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         287
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         358
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         395
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         429..431
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
SQ   SEQUENCE   450 AA;  50313 MW;  080DF5EC0D4AD521 CRC64;
     MTSWNFVCLS LGSNLGNRHE HIRRAYASLK KAGIRNLKSS VILETKALLL EGAPKEWDLP
     YFNSVVIGET QLSPDELIEE IKMIESRFGQ DASLKWGPRP IDIDVLFYGD EAFSYHSDKC
     TIPHPKVLER PFLLSMIASL CPYRRFRLEG SSCNGKTFAE LAAIYPLTEE DALGSFGSAT
     QIMGIVNITD NSISDTGLFL EARRAAAHAE RLFAEGASII DLGAQATNPR VKDLGSVEQE
     WERLEPVLRL LAERWGAAQQ CPDVSIDTFR PEIIRRAVEV FPIRWINDVS GGSLEMAHLA
     KEFGLRLLIN HSCSLPPRPD CVLSYEESPI EQMLRWGESQ LEQFAQVGLD TSWQVVFDPG
     IGFGKTPVQS MLLMDGVKQF KRVLECPVLI GHSRKSCLSM LGRFNSNDRD WETIGCSVSL
     HDRGVDYLRV HQVEGNRRAL AAAAWAGMFV
//