ID C2MES2_BACCE Unreviewed; 112 AA. AC C2MES2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 14-DEC-2022, entry version 34. DE RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079}; DE EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079}; GN ORFNames=bcere0001_610 {ECO:0000313|EMBL:EEK47068.1}; OS Bacillus cereus m1293. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526973 {ECO:0000313|EMBL:EEK47068.1}; RN [1] {ECO:0000313|EMBL:EEK47068.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M1293 {ECO:0000313|EMBL:EEK47068.1}; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). 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|ARBA:ARBA00001353, CC 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|ARBA:ARBA00005013, 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:EEK47068.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ACLS01000002; EEK47068.1; -; Genomic_DNA. DR AlphaFoldDB; C2MES2; -. DR EnsemblBacteria; EEK47068; EEK47068; bcere0001_610. DR HOGENOM; CLU_112632_1_3_9; -. DR UniPathway; UPA00077; UER00154. DR Proteomes; UP000002290; 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 PANTHER; PTHR42844; DIHYDRONEOPTERIN ALDOLASE 1-RELATED; 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 {ECO:0000256|RuleBase:RU362079}; KW Lyase {ECO:0000256|RuleBase:RU362079}. FT DOMAIN 1..109 FT /note="FolB" FT /evidence="ECO:0000259|SMART:SM00905" SQ SEQUENCE 112 AA; 12930 MW; A28FFB026C50F612 CRC64; MEFYGYHGVF PEENKLGQRF KVDLTVELDL KQAGESDDLE HSVNYGELFE LCRKVVEDRT YKLVESIAEN IATDILKQYE SISRCTIKVI KPDPPIPGHY RAVAVEITRE RP //