FOLKP_CHLMU
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 03-AUG-2022, entry version 130.
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; Chlamydiae; 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_CP027217.1.
DR AlphaFoldDB; P82602; -.
DR SMR; P82602; -.
DR STRING; 243161.TC_0903; -.
DR EnsemblBacteria; AAF39696; AAF39696; TC_0903.
DR GeneID; 1246272; -.
DR KEGG; cmu:TC_0903; -.
DR eggNOG; COG0294; Bacteria.
DR eggNOG; COG0801; Bacteria.
DR HOGENOM; CLU_008023_2_2_0; -.
DR OMA; HIMAILN; -.
DR OrthoDB; 1275854at2; -.
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; 3.20.20.20; -; 1.
DR Gene3D; 3.30.70.560; -; 1.
DR InterPro; IPR045031; DHP_synth.
DR InterPro; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
DR PANTHER; PTHR20941; PTHR20941; 1.
DR Pfam; PF01288; HPPK; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR SUPFAM; SSF55083; SSF55083; 1.
DR TIGRFAMs; TIGR01496; DHPS; 1.
DR TIGRFAMs; TIGR01498; folK; 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
