ID   FOLB_SYNY3              Reviewed;         118 AA.
AC   P74342;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 115.
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=slr1626;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAA18436.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000022; BAA18436.1; ALT_INIT; Genomic_DNA.
DR   PIR; S76177; S76177.
DR   AlphaFoldDB; P74342; -.
DR   SMR; P74342; -.
DR   IntAct; P74342; 4.
DR   STRING; 1148.1653523; -.
DR   PaxDb; P74342; -.
DR   PRIDE; P74342; -.
DR   EnsemblBacteria; BAA18436; BAA18436; BAA18436.
DR   KEGG; syn:slr1626; -.
DR   eggNOG; COG1539; Bacteria.
DR   InParanoid; P74342; -.
DR   OMA; GHYKSVA; -.
DR   PhylomeDB; P74342; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000001425; 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   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..118
FT                   /note="Probable dihydroneopterin aldolase"
FT                   /id="PRO_0000168293"
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   118 AA;  13146 MW;  C1D719A2ADFA40CD CRC64;
     MDTLNVKGIR AYGYTGYFDA EQFLGQWFEV DLTIWIDLAK AGQSDDLNDT LNYADAVAIV
     QKLIRESKFK MIEKLAEAIA DAILGTGKTQ QVKVALTKCQ APIPDFDGDV TLEILRSR