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Database: UniProt
Entry: B0JMU9_MICAN
LinkDB: B0JMU9_MICAN
Original site: B0JMU9_MICAN 
ID   B0JMU9_MICAN            Unreviewed;       118 AA.
AC   B0JMU9;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE            EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN   OrderedLocusNames=MAE_02910 {ECO:0000313|EMBL:BAG00113.1};
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447 {ECO:0000313|EMBL:BAG00113.1, ECO:0000313|Proteomes:UP000001510};
RN   [1] {ECO:0000313|EMBL:BAG00113.1, ECO:0000313|Proteomes:UP000001510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 {ECO:0000313|EMBL:BAG00113.1,
RC   ECO:0000313|Proteomes:UP000001510};
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(2007).
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}.
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DR   EMBL; AP009552; BAG00113.1; -; Genomic_DNA.
DR   RefSeq; WP_002795705.1; NC_010296.1.
DR   AlphaFoldDB; B0JMU9; -.
DR   STRING; 449447.MAE_02910; -.
DR   PaxDb; 449447-MAE_02910; -.
DR   EnsemblBacteria; BAG00113; BAG00113; MAE_02910.
DR   KEGG; mar:MAE_02910; -.
DR   PATRIC; fig|449447.4.peg.275; -.
DR   eggNOG; COG1539; Bacteria.
DR   HOGENOM; CLU_112632_1_4_3; -.
DR   OMA; GHYKSVA; -.
DR   BioCyc; MAER449447:MAE_RS01315-MONOMER; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000001510; Chromosome.
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   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   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..116
FT                   /note="Dihydroneopterin aldolase/epimerase"
FT                   /evidence="ECO:0000259|SMART:SM00905"
SQ   SEQUENCE   118 AA;  13343 MW;  8E652D0A3A4017EC CRC64;
     MDTIHFTGIR AYGYTGYLAE EQVLGQWFEV DLSLELDISI AGKSDAIEDT LDYRQAIKIV
     KHQIETSKFA LVEKLATVIA EDILQLDRVR QVRVQLSKPA APIPHFTGKI TIDITRSR
//
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