ID   Q4FPI2_PELUB            Unreviewed;       141 AA.
AC   Q4FPI2;
DT   30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2005, sequence version 1.
DT   02-SEP-2026, entry version 84.
DE   RecName: Full=dihydroneopterin aldolase {ECO:0000256|ARBA:ARBA00013043};
DE            EC=4.1.2.25 {ECO:0000256|ARBA:ARBA00013043};
DE   AltName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|ARBA:ARBA00032903};
GN   Name=folB {ECO:0000313|EMBL:AAZ20907.1};
GN   OrderedLocusNames=SAR11_0083 {ECO:0000313|EMBL:AAZ20907.1};
OS   Pelagibacter ubique (strain HTCC1062).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Candidatus Pelagibacterales; Candidatus Pelagibacteraceae;
OC   Candidatus Pelagibacter.
OX   NCBI_TaxID=335992 {ECO:0000313|EMBL:AAZ20907.1, ECO:0000313|Proteomes:UP000002528};
RN   [1] {ECO:0000313|EMBL:AAZ20907.1, ECO:0000313|Proteomes:UP000002528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC1062 {ECO:0000313|EMBL:AAZ20907.1,
RC   ECO:0000313|Proteomes:UP000002528};
RX   PubMed=16109880; DOI=10.1126/science.1114057;
RA   Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA   Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA   Carrington J.C., Mathur E.J.;
RT   "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL   Science 309:1242-1245(2005).
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:0000256|ARBA:ARBA00001353};
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       {ECO:0000256|ARBA:ARBA00005013}.
CC   -!- SIMILARITY: Belongs to the DHNA family.
CC       {ECO:0000256|ARBA:ARBA00005708}.
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DR   EMBL; CP000084; AAZ20907.1; -; Genomic_DNA.
DR   RefSeq; WP_011281463.1; NC_007205.1.
DR   AlphaFoldDB; Q4FPI2; -.
DR   STRING; 335992.SAR11_0083; -.
DR   GeneID; 66294586; -.
DR   KEGG; pub:SAR11_0083; -.
DR   eggNOG; COG1539; Bacteria.
DR   HOGENOM; CLU_112632_0_2_5; -.
DR   OrthoDB; 5297888at2; -.
DR   Proteomes; UP000002528; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006760; P:folic acid-containing compound metabolic process; IEA:InterPro.
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   NCBIfam; TIGR00526; folB_dom; 1.
DR   PANTHER; PTHR42844; DIHYDRONEOPTERIN ALDOLASE 1-RELATED; 1.
DR   PANTHER; PTHR42844:SF1; DIHYDRONEOPTERIN ALDOLASE 1-RELATED; 1.
DR   Pfam; PF02152; FolB; 1.
DR   SMART; SM00905; FolB; 1.
DR   SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AAZ20907.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002528}.
FT   DOMAIN          24..134
FT                   /note="Dihydroneopterin aldolase/epimerase"
FT                   /evidence="ECO:0000259|SMART:SM00905"
SQ   SEQUENCE   141 AA;  16701 MW;  FDA257712BF8134D CRC64;
     MKKTNLNIIK IDKNKSLFNY EKKILIKELT LDLKLGYYDF EKEKTQKVKF SLEIDYEDRK
     PTNDKDIKSI VNYGQVVKLI TKLAKNKHYN FLETLAEDVF DVLFKDKRIG KIMLQIEKLE
     IIKECASVGI QITKKRSHEE L
//