ID   FOLB_MYCLE              Reviewed;         132 AA.
AC   O69529;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Dihydroneopterin aldolase;
DE            Short=DHNA;
DE            EC=4.1.2.25 {ECO:0000250|UniProtKB:P9WNC5};
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:P9WNC5};
DE   AltName: Full=7,8-dihydroneopterin hydroxylase;
DE            EC=1.13.11.81 {ECO:0000250|UniProtKB:P9WNC5};
DE   AltName: Full=Dihydroneopterin epimerase;
DE   AltName: Full=Dihydroneopterin hydroxylase;
GN   Name=folB; OrderedLocusNames=ML0225; ORFNames=MLCB2548.06c;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC       hydroxymethyl-7,8-dihydropterin, 7,8-dihydromonapterin and 7,8-
CC       dihydroxanthopterin, respectively, in equal quantities. After longer
CC       incubation times the only product is 6-hydroxymethyl-7,8-dihydropterin.
CC       {ECO:0000250|UniProtKB:P9WNC5}.
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:P9WNC5};
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:P9WNC5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,8-dihydroneopterin + O2 = 7,8-dihydroxanthopterin + formate
CC         + glycolaldehyde + H(+); Xref=Rhea:RHEA:45332, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17001,
CC         ChEBI:CHEBI:17071, ChEBI:CHEBI:85130; EC=1.13.11.81;
CC         Evidence={ECO:0000250|UniProtKB:P9WNC5};
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; AL023093; CAA18793.1; -; Genomic_DNA.
DR   EMBL; AL583917; CAC29733.1; -; Genomic_DNA.
DR   PIR; A86937; A86937.
DR   RefSeq; NP_301285.1; NC_002677.1.
DR   RefSeq; WP_010907609.1; NC_002677.1.
DR   AlphaFoldDB; O69529; -.
DR   SMR; O69529; -.
DR   STRING; 272631.ML0225; -.
DR   EnsemblBacteria; CAC29733; CAC29733; CAC29733.
DR   KEGG; mle:ML0225; -.
DR   PATRIC; fig|272631.5.peg.357; -.
DR   Leproma; ML0225; -.
DR   eggNOG; COG1539; Bacteria.
DR   HOGENOM; CLU_112632_1_1_11; -.
DR   OMA; GHYKSVA; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000000806; 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:0016491; F:oxidoreductase 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; Oxidoreductase; Reference proteome.
FT   CHAIN           1..132
FT                   /note="Dihydroneopterin aldolase"
FT                   /id="PRO_0000168274"
FT   ACT_SITE        99
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC16"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC16"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC16"
FT   BINDING         73..74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC16"
SQ   SEQUENCE   132 AA;  14449 MW;  B93663D838044DD0 CRC64;
     MADRMELRGL IVRGRHGVYE VERANGQDFI VDVILWIDLA DAAANDNLAD TYDYVVLAER
     TAAIIAGPPR NLIETVGSEI ADFVMDDERV HAVEVVVHKP QAPIPQQFSD VAVVVRRSRR
     GGRGSMIPAS GV