ID   FOLB_STAAW              Reviewed;         121 AA.
AC   P64147; Q99W88;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Dihydroneopterin aldolase;
DE            Short=DHNA;
DE            EC=4.1.2.25 {ECO:0000250|UniProtKB:P0AC16};
DE   AltName: Full=7,8-dihydroneopterin 2'-epimerase;
DE   AltName: Full=7,8-dihydroneopterin aldolase;
DE   AltName: Full=7,8-dihydroneopterin epimerase;
DE            EC=5.1.99.8 {ECO:0000250|UniProtKB:P0AC16};
DE   AltName: Full=Dihydroneopterin epimerase;
GN   Name=folB; OrderedLocusNames=MW0470;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC       hydroxymethyl-7,8-dihydropterin. Can also catalyze the epimerization of
CC       carbon 2' of dihydroneopterin to dihydromonapterin.
CC       {ECO:0000250|UniProtKB:P56740}.
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:P56740};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,8-dihydroneopterin = 7,8-dihydromonapterin;
CC         Xref=Rhea:RHEA:45328, ChEBI:CHEBI:17001, ChEBI:CHEBI:71175;
CC         EC=5.1.99.8; 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   -!- SUBUNIT: Homooctamer. Four molecules assemble into a ring, and two
CC       rings come together to give a cylinder with a hole of at least 13 a
CC       diameter (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000305}.
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DR   EMBL; BA000033; BAB94335.1; -; Genomic_DNA.
DR   RefSeq; WP_001154302.1; NC_003923.1.
DR   AlphaFoldDB; P64147; -.
DR   BMRB; P64147; -.
DR   SMR; P64147; -.
DR   EnsemblBacteria; BAB94335; BAB94335; BAB94335.
DR   KEGG; sam:MW0470; -.
DR   HOGENOM; CLU_112632_1_3_9; -.
DR   OMA; GHYKSVA; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; Isomerase; Lyase.
FT   CHAIN           1..121
FT                   /note="Dihydroneopterin aldolase"
FT                   /id="PRO_0000168282"
FT   ACT_SITE        100
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P56740"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P56740"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P56740"
FT   BINDING         73..74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P56740"
SQ   SEQUENCE   121 AA;  13735 MW;  55AC781A97D5DC6D CRC64;
     MQDTIFLKGM RFYGYHGALS AENEIGQIFK VDVTLKVDLA EAGRTDNVID TVHYGEVFEE
     VKSIMEGKAV NLLEHLAERI ANRINSQYNR VMETKVRITK ENPPIPGHYD GVGIEIVREN
     K