ID   FOLKP_CHLMU             Reviewed;         450 AA.
AC   P82602;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 138.
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=TC_0903;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39696.1; -; Genomic_DNA.
DR   PIR; G81652; G81652.
DR   RefSeq; WP_010231893.1; NZ_CP063055.1.
DR   AlphaFoldDB; P82602; -.
DR   SMR; P82602; -.
DR   GeneID; 1246272; -.
DR   KEGG; cmu:TC_0903; -.
DR   eggNOG; COG0294; Bacteria.
DR   eggNOG; COG0801; Bacteria.
DR   HOGENOM; CLU_008023_2_2_0; -.
DR   OrthoDB; 9811744at2; -.
DR   UniPathway; UPA00077; UER00155.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000000800; Chromosome.
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; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
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; Transferase.
FT   CHAIN           1..450
FT                   /note="Folate synthesis bifunctional protein"
FT                   /id="PRO_0000168239"
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;  50448 MW;  068BE8D2DCEE4A2E CRC64;
     MTTWNFVCLG LGSNLGNRHE YIKRAYESLK KAGIRNLKSS VILETKALLL EGSPKEWDLP
     YFNCVAIGET QLSPDELVKE IKMIENRLSR DSSLKWGPRS IDIDVLLYGD ESYSCCSERC
     IIPHPRLLER PFLLSMMASL CPYRYFRLRG SPYDGKTFAE LAAIYPLTEK DVLGSFAPTT
     QIMGIVNVTD DSISDTGLFL EAKRAAAHAE RLFAEGASII DLGAQATNPR VRDLGSVEQE
     WERLEPVLQI LAESWKDAKQ YPDVSIDTFR PEVIRRAIQV FPIRWINDVS GGSLEMAHLA
     KDLGLRLLIN HSCSLPPRPD CVLSYEESPV TQMLRWGESQ LETFAQIGLD TSWQVVFDPG
     IGFGKTPVQS MQLMEGVAKF KHILKCPVLI GHSRKSCLSL LGRFSSQDRD WETIGCSVAL
     HNQGVDYLRV HQVEGNRRVL AAAAWSGMPV
//