SULD_STRR6
ID SULD_STRR6 Reviewed; 270 AA.
AC P59657;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Bifunctional folate synthesis protein;
DE Includes:
DE RecName: Full=Dihydroneopterin aldolase {ECO:0000303|PubMed:16781731};
DE Short=DHNA {ECO:0000303|PubMed:16781731};
DE EC=4.1.2.25;
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;
DE AltName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000303|PubMed:16781731};
DE Short=PPPK;
DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase;
DE Short=HPPK {ECO:0000303|PubMed:16781731};
GN Name=sulD {ECO:0000303|PubMed:16781731}; OrderedLocusNames=spr0269;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), AND SUBUNIT.
RX PubMed=16781731; DOI=10.1016/j.jmb.2006.05.038;
RA Garcon A., Levy C., Derrick J.P.;
RT "Crystal structure of the bifunctional dihydroneopterin aldolase/6-
RT hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Streptococcus
RT pneumoniae.";
RL J. Mol. Biol. 360:644-653(2006).
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:0000250|UniProtKB:P22291}.
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:0000250|UniProtKB:P22291};
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:0000250|UniProtKB:P22291};
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: Homooctamer. {ECO:0000269|PubMed:16781731}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE007317; AAK99073.1; -; Genomic_DNA.
DR RefSeq; NP_357863.1; NC_003098.1.
DR RefSeq; WP_000372525.1; NC_003098.1.
DR PDB; 2CG8; X-ray; 2.90 A; A/B/C/D=1-270.
DR PDBsum; 2CG8; -.
DR AlphaFoldDB; P59657; -.
DR SMR; P59657; -.
DR STRING; 171101.spr0269; -.
DR EnsemblBacteria; AAK99073; AAK99073; spr0269.
DR GeneID; 60233326; -.
DR KEGG; spr:spr0269; -.
DR PATRIC; fig|171101.6.peg.306; -.
DR eggNOG; COG0801; Bacteria.
DR eggNOG; COG1539; Bacteria.
DR HOGENOM; CLU_023499_0_0_9; -.
DR OMA; IKKPWAP; -.
DR UniPathway; UPA00077; UER00154.
DR UniPathway; UPA00077; UER00155.
DR EvolutionaryTrace; P59657; -.
DR Proteomes; UP000000586; 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 3D-structure; ATP-binding; Folate biosynthesis; Kinase; Lyase; Magnesium;
KW Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..270
FT /note="Bifunctional folate synthesis protein"
FT /id="PRO_0000168245"
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 STRAND 2..13
FT /evidence="ECO:0007829|PDB:2CG8"
FT HELIX 19..24
FT /evidence="ECO:0007829|PDB:2CG8"
FT STRAND 26..36
FT /evidence="ECO:0007829|PDB:2CG8"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:2CG8"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:2CG8"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:2CG8"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:2CG8"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:2CG8"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:2CG8"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2CG8"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:2CG8"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:2CG8"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:2CG8"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:2CG8"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:2CG8"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2CG8"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:2CG8"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:2CG8"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:2CG8"
FT HELIX 261..265
FT /evidence="ECO:0007829|PDB:2CG8"
SQ SEQUENCE 270 AA; 31097 MW; B3CD87345848C584 CRC64;
MDQLQIKDLE MFAYHGLFPS EKELGQKFIV SAILSYDMTK AATDLDLTAS VHYGELCQQW
TTWFQETSED LIETVAYKLV ERTFESYPLV QEMKLELKKP WAPVHLSLDT CSVTIHRRKQ
RAFIALGSNM GDKQANLKQA IDKLRARGIH ILKESSVLAT EPWGGVEQDS FANQVVEVET
WLPAQDLLET LLAIESELGR VREVHWGPRL IDLDLLFVED QILYTDDLIL PHPYIAERLF
VLESLQEIAP HFIHPILKQP IRNLYDALKK
