ID   FOLB_STRPY              Reviewed;         119 AA.
AC   P0C0G4; O33725; P0A3E1;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Dihydroneopterin aldolase;
DE            Short=DHNA;
DE            EC=4.1.2.25;
DE   AltName: Full=7,8-dihydroneopterin aldolase;
GN   Name=folB; Synonyms=folQ;
OS   Streptococcus pyogenes.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G56;
RX   PubMed=9593127; DOI=10.1128/aac.42.5.1062;
RA   Swedberg G., Ringertz S., Skoeld O.;
RT   "Sulfonamide resistance in Streptococcus pyogenes is associated with
RT   differences in the amino acid sequence of its chromosomal dihydropteroate
RT   synthase.";
RL   Antimicrob. Agents Chemother. 42:1062-1067(1998).
CC   -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC       hydroxymethyl-7,8-dihydropterin. {ECO:0000250|UniProtKB:P0AC16}.
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:P0AC16};
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   -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000305}.
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DR   EMBL; AJ000685; CAA04239.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C0G4; -.
DR   SMR; P0C0G4; -.
DR   eggNOG; COG1539; Bacteria.
DR   UniPathway; UPA00077; UER00154.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00534; DHNA_DHNTPE; 1.
DR   Gene3D; 3.30.1130.10; -; 1.
DR   InterPro; IPR006156; Dihydroneopterin_aldolase.
DR   InterPro; IPR006157; FolB_dom.
DR   InterPro; IPR043133; GTP-CH-I_C/QueF.
DR   PANTHER; PTHR42844; PTHR42844; 1.
DR   Pfam; PF02152; FolB; 1.
DR   SMART; SM00905; FolB; 1.
DR   TIGRFAMs; TIGR00525; folB; 1.
DR   TIGRFAMs; TIGR00526; folB_dom; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis; Lyase.
FT   CHAIN           1..119
FT                   /note="Dihydroneopterin aldolase"
FT                   /id="PRO_0000168288"
FT   ACT_SITE        99
FT                   /note="Proton donor/acceptor"
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"
SQ   SEQUENCE   119 AA;  13316 MW;  3D0289F2E33FE7A9 CRC64;
     MDKIVLEGCR FYGYHGAYKE EQTLGQIFLV DLELSVDLQA ASLSSQLTDT VHYGMVFDSV
     RQLVEGEKFI LIDGLAGAIC EQLFNEFPPI EAIKVAIKKE NPPIAGHYKA VGIELERQR