FOLB_STAES
ID FOLB_STAES Reviewed; 121 AA.
AC Q8CMT8;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=SE_2268;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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}.
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; AE015929; AAO05910.1; -; Genomic_DNA.
DR RefSeq; NP_765823.1; NC_004461.1.
DR RefSeq; WP_001832204.1; NZ_WBME01000023.1.
DR AlphaFoldDB; Q8CMT8; -.
DR SMR; Q8CMT8; -.
DR STRING; 176280.SE_2268; -.
DR EnsemblBacteria; AAO05910; AAO05910; SE_2268.
DR GeneID; 50019574; -.
DR KEGG; sep:SE_2268; -.
DR PATRIC; fig|176280.10.peg.2211; -.
DR eggNOG; COG1539; Bacteria.
DR HOGENOM; CLU_112632_1_3_9; -.
DR OMA; GHYKSVA; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000001411; 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_0000168284"
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; 13694 MW; E9963A5D126D5EB7 CRC64;
MNDIIFLNGM RFYGYHGVLA AENDIGQIFV VDITLKVDLS YAGQSDDVKD TVNYGEVYKD
VKSIVEGPRS CLIEHLAERI AKHINSHYNR VMETKVRITK ENPPIPGHYD GVGIEIVREN
D
