ID   FOLB_STRCO              Reviewed;         119 AA.
AC   Q9X8I0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Dihydroneopterin aldolase;
DE            Short=DHNA;
DE            EC=4.1.2.25;
DE   AltName: Full=7,8-dihydroneopterin aldolase;
GN   Name=folB; OrderedLocusNames=SCO3400; ORFNames=SCE9.07;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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}.
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; AL939116; CAB42753.1; -; Genomic_DNA.
DR   PIR; T36326; T36326.
DR   RefSeq; NP_627606.1; NC_003888.3.
DR   RefSeq; WP_011028954.1; NZ_VNID01000023.1.
DR   AlphaFoldDB; Q9X8I0; -.
DR   SMR; Q9X8I0; -.
DR   STRING; 100226.SCO3400; -.
DR   GeneID; 1098837; -.
DR   KEGG; sco:SCO3400; -.
DR   PATRIC; fig|100226.15.peg.3463; -.
DR   eggNOG; COG1539; Bacteria.
DR   HOGENOM; CLU_112632_1_1_11; -.
DR   InParanoid; Q9X8I0; -.
DR   OMA; GHYKSVA; -.
DR   PhylomeDB; Q9X8I0; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IBA:GO_Central.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
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; Reference proteome.
FT   CHAIN           1..119
FT                   /note="Dihydroneopterin aldolase"
FT                   /id="PRO_0000168287"
FT   ACT_SITE        98
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;  13002 MW;  0E865735FA1A694D CRC64;
     MDRVALRGLK ARGHHGVFPK EREDGQTFLV DIVLGLDTRP AAADDDLAKT VHYGIVAEEV
     VAVVEGEPVN LVETLAERIA QVCLKHEGVE EVEVCVHKPD APITVPFDDV TVTIIRSRV