ID   FOLB_CHLTR              Reviewed;         124 AA.
AC   O84620;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Probable dihydroneopterin aldolase;
DE            Short=DHNA;
DE            EC=4.1.2.25;
DE   AltName: Full=7,8-dihydroneopterin aldolase;
GN   Name=folB; OrderedLocusNames=CT_614;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
CC   -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC       hydroxymethyl-7,8-dihydropterin. {ECO:0000250}.
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   -!- 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; AE001273; AAC68217.1; -; Genomic_DNA.
DR   PIR; B71494; B71494.
DR   RefSeq; NP_220131.1; NC_000117.1.
DR   RefSeq; WP_009871982.1; NC_000117.1.
DR   AlphaFoldDB; O84620; -.
DR   SMR; O84620; -.
DR   STRING; 813.O172_03355; -.
DR   EnsemblBacteria; AAC68217; AAC68217; CT_614.
DR   GeneID; 884397; -.
DR   KEGG; ctr:CT_614; -.
DR   PATRIC; fig|272561.5.peg.671; -.
DR   HOGENOM; CLU_112632_3_0_0; -.
DR   InParanoid; O84620; -.
DR   OMA; QIGSACF; -.
DR   BioCyc; MetaCyc:MON-18793; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000000431; 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   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   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..124
FT                   /note="Probable dihydroneopterin aldolase"
FT                   /id="PRO_0000168268"
FT   ACT_SITE        103
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC16"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC16"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC16"
FT   BINDING         75..76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC16"
SQ   SEQUENCE   124 AA;  13941 MW;  9755847F2DEAA3D8 CRC64;
     MLLYRLDIAD FRVWVSIGVS EQERHYPQPV LVSLSLFFKE EPKACSTDKV SDSVCYAELV
     SLIEEVATNN PCALIERLAK VLLEKIEKAL AGQVSRIDLR VSKERPPIPD LLSPVSFSIS
     REVP