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Database: UniProt
Entry: A0A0S8K494_9BACE
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Original site: A0A0S8K494_9BACE 
ID   A0A0S8K494_9BACE        Unreviewed;       117 AA.
AC   A0A0S8K494;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE            EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN   ORFNames=AMS26_05410 {ECO:0000313|EMBL:KPL16195.1};
OS   Bacteroides sp. SM23_62.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1703352 {ECO:0000313|EMBL:KPL16195.1, ECO:0000313|Proteomes:UP000050819};
RN   [1] {ECO:0000313|EMBL:KPL16195.1, ECO:0000313|Proteomes:UP000050819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_62 {ECO:0000313|EMBL:KPL16195.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC       hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.
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|RuleBase:RU362079};
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|RuleBase:RU362079}.
CC   -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000256|ARBA:ARBA00005708,
CC       ECO:0000256|RuleBase:RU362079}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPL16195.1}.
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DR   EMBL; LJUP01000034; KPL16195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8K494; -.
DR   PATRIC; fig|1703352.3.peg.2106; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000050819; Unassembled WGS sequence.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
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; TIGR00525; folB; 1.
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|RuleBase:RU362079};
KW   Lyase {ECO:0000256|RuleBase:RU362079}.
FT   DOMAIN          4..117
FT                   /note="Dihydroneopterin aldolase/epimerase"
FT                   /evidence="ECO:0000259|SMART:SM00905"
SQ   SEQUENCE   117 AA;  13385 MW;  BD36877620B7C774 CRC64;
     MGLIQIENME FYAFHGHYRE EQIVGNKFLV DLSIDSDMSV PAASDNLKDA INYQRAYKLV
     KEEMEKKSKL LENIAKRILD TIYDNFDGIR EVTVKVSKMN PPMGGGRIEK VSVTLSR
//
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