ID   FOLB_ECOL6              Reviewed;         122 AA.
AC   P0AC17; P31055; P76659;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Dihydroneopterin aldolase;
DE            Short=DHNA;
DE            EC=4.1.2.25 {ECO:0000250|UniProtKB:P0AC16};
DE   AltName: Full=7,8-dihydroneopterin 2'-epimerase;
DE   AltName: Full=7,8-dihydroneopterin aldolase;
DE   AltName: Full=7,8-dihydroneopterin epimerase;
DE            EC=5.1.99.8 {ECO:0000250|UniProtKB:P0AC16};
DE   AltName: Full=Dihydroneopterin epimerase;
GN   Name=folB; OrderedLocusNames=c3808;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC       hydroxymethyl-7,8-dihydropterin. Can use L-threo-dihydroneopterin and
CC       D-erythro-dihydroneopterin as substrates for the formation of 6-
CC       hydroxymethyldihydropterin, but it can also catalyze the epimerization
CC       of carbon 2' of dihydroneopterin to dihydromonapterin at appreciable
CC       velocity. {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   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,8-dihydroneopterin = 7,8-dihydromonapterin;
CC         Xref=Rhea:RHEA:45328, ChEBI:CHEBI:17001, ChEBI:CHEBI:71175;
CC         EC=5.1.99.8; 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   -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN82253.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN82253.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001295541.1; NC_004431.1.
DR   AlphaFoldDB; P0AC17; -.
DR   SMR; P0AC17; -.
DR   STRING; 199310.c3808; -.
DR   EnsemblBacteria; AAN82253; AAN82253; c3808.
DR   GeneID; 67414995; -.
DR   KEGG; ecc:c3808; -.
DR   eggNOG; COG1539; Bacteria.
DR   HOGENOM; CLU_112632_0_2_6; -.
DR   OMA; GIYEWEK; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; Isomerase; Lyase.
FT   CHAIN           1..122
FT                   /note="Dihydroneopterin aldolase"
FT                   /id="PRO_0000168270"
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   122 AA;  13620 MW;  BEA82C1E0AA38A55 CRC64;
     MDIVFIEQLS VITTIGVYDW EQTIEQKLVF DIEMAWDNRK AAKSDDVADC LSYADIAETV
     VSHVEGARFA LVERVAEEVA ELLLARFNSP WVRIKLSKPG AVARAANVGV IIERGNNLKE
     NN