SULD_STRPN
ID SULD_STRPN Reviewed; 270 AA.
AC P22291; O33697;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Bifunctional folate synthesis protein;
DE Includes:
DE RecName: Full=Dihydroneopterin aldolase {ECO:0000303|PubMed:8385663};
DE Short=DHNA {ECO:0000303|PubMed:8385663};
DE EC=4.1.2.25 {ECO:0000269|PubMed:8385663};
DE AltName: Full=7,8-dihydroneopterin aldolase;
DE Includes:
DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase;
DE EC=2.7.6.3 {ECO:0000269|PubMed:2168367, ECO:0000269|PubMed:8385663};
DE AltName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000303|PubMed:2168367};
DE Short=PPPK {ECO:0000303|PubMed:2168367};
DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase;
DE Short=HPPK {ECO:0000303|PubMed:8385663};
GN Name=sulD {ECO:0000303|PubMed:2168367}; OrderedLocusNames=SP_0292;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-13, CATALYTIC
RP ACTIVITY, AND SUBUNIT.
RC STRAIN=708;
RX PubMed=2168367; DOI=10.1128/jb.172.9.4766-4774.1990;
RA Lopez P., Greenberg B., Lacks S.A.;
RT "DNA sequence of folate biosynthesis gene sulD, encoding
RT hydroxymethyldihydropterin pyrophosphokinase in Streptococcus pneumoniae,
RT and characterization of the enzyme.";
RL J. Bacteriol. 172:4766-4774(1990).
RN [2]
RP SEQUENCE REVISION TO 156-170.
RC STRAIN=772;
RX PubMed=7798151; DOI=10.1128/jb.177.1.66-74.1995;
RA Lacks S.A., Greenberg B., Lopez P.;
RT "A cluster of four genes encoding enzymes for five steps in the folate
RT biosynthetic pathway of Streptococcus pneumoniae.";
RL J. Bacteriol. 177:66-74(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND CHARACTERIZATION.
RX PubMed=8385663; DOI=10.1128/jb.175.8.2214-2220.1993;
RA Lopez P., Lacks S.A.;
RT "A bifunctional protein in the folate biosynthetic pathway of Streptococcus
RT pneumoniae with dihydroneopterin aldolase and hydroxymethyldihydropterin
RT pyrophosphokinase activities.";
RL J. Bacteriol. 175:2214-2220(1993).
CC -!- FUNCTION: Catalyzes two sequential steps of tetrahydrofolate
CC biosynthesis, the conversion of 7,8-dihydroneopterin to 6-
CC hydroxymethyl-7,8-dihydropterin diphosphate.
CC {ECO:0000269|PubMed:8385663}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin +
CC glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001,
CC ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25;
CC Evidence={ECO:0000269|PubMed:8385663};
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 Evidence={ECO:0000269|PubMed:2168367, ECO:0000269|PubMed:8385663};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 3/4.
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 -!- SUBUNIT: Homotrimer or homotetramer. {ECO:0000269|PubMed:2168367,
CC ECO:0000269|PubMed:8385663}.
CC -!- INTERACTION:
CC P22291; Q97NV3: groES; NbExp=2; IntAct=EBI-2207011, EBI-2206949;
CC -!- SIMILARITY: In the N-terminal section; belongs to the DHNA family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the HPPK family.
CC {ECO:0000305}.
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DR EMBL; U16156; AAB63947.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK74470.1; -; Genomic_DNA.
DR PIR; A36704; A36704.
DR PIR; E95034; E95034.
DR PIR; E97905; E97905.
DR RefSeq; WP_000372529.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P22291; -.
DR SMR; P22291; -.
DR IntAct; P22291; 1.
DR STRING; 170187.SP_0292; -.
DR EnsemblBacteria; AAK74470; AAK74470; SP_0292.
DR KEGG; spn:SP_0292; -.
DR eggNOG; COG0801; Bacteria.
DR eggNOG; COG1539; Bacteria.
DR OMA; IKKPWAP; -.
DR PhylomeDB; P22291; -.
DR BioCyc; SPNE170187:G1FZB-301-MON; -.
DR UniPathway; UPA00077; UER00154.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000000585; 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:0004150; F:dihydroneopterin aldolase 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; cd00534; DHNA_DHNTPE; 1.
DR CDD; cd00483; HPPK; 1.
DR Gene3D; 3.30.1130.10; -; 1.
DR Gene3D; 3.30.70.560; -; 1.
DR InterPro; IPR006156; Dihydroneopterin_aldolase.
DR InterPro; IPR006157; FolB_dom.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR Pfam; PF02152; FolB; 1.
DR Pfam; PF01288; HPPK; 1.
DR SMART; SM00905; FolB; 1.
DR SUPFAM; SSF55083; SSF55083; 1.
DR TIGRFAMs; TIGR00525; folB; 1.
DR TIGRFAMs; TIGR00526; folB_dom; 1.
DR TIGRFAMs; TIGR01498; folK; 1.
DR PROSITE; PS00794; HPPK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Folate biosynthesis; Kinase; Lyase;
KW Magnesium; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..270
FT /note="Bifunctional folate synthesis protein"
FT /id="PRO_0000168244"
FT REGION 1..119
FT /note="DHNA"
FT REGION 120..270
FT /note="HPPK"
FT ACT_SITE 99
FT /note="Proton donor/acceptor; for DHNA activity"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 72..73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 160..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26281"
FT BINDING 171..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26281"
FT BINDING 192..195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26281"
FT BINDING 200..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26281"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P26281"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P26281"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P26281"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P26281"
FT BINDING 227..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26281"
FT BINDING 238..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26281"
FT CONFLICT 29
FT /note="V -> I (in Ref. 1; AAB63947)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="F -> S (in Ref. 1; AAB63947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 31143 MW; 1AAD0229E639A827 CRC64;
MDQLQIKDLE MFAYHGLFPS EKELGQKFVV SAILSYDMTK AATDLDLTAS VHYGELCQQW
TTWFQETSED LIETVAYKLV ERTFEFYPLV QEMKLELKKP WAPVHLSLDT CSVTIHRRKQ
RAFIALGSNM GDKQANLKQA IDKLRARGIH ILKESSVLAT EPWGGVEQDS FANQVVEVET
WLPAQDLLET LLAIESELGR VREVHWGPRL IDLDLLFVED QILYTDDLIL PHPYIAERLF
VLESLQEIAP HFIHPILKQP IRNLYDALKK
