ID FOLB_STAAC Reviewed; 121 AA.
AC Q5HIG0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
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=SACOL0559;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW37671.1; -; Genomic_DNA.
DR RefSeq; WP_001154302.1; NC_002951.2.
DR AlphaFoldDB; Q5HIG0; -.
DR BMRB; Q5HIG0; -.
DR SMR; Q5HIG0; -.
DR KEGG; sac:SACOL0559; -.
DR HOGENOM; CLU_112632_1_3_9; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000000530; 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 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; Isomerase; Lyase.
FT CHAIN 1..121
FT /note="Dihydroneopterin aldolase"
FT /id="PRO_0000168277"
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
//
