FOLB_STAHA
ID FOLB_STAHA Reviewed; 84 AA.
AC Q59920;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 74.
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;
DE Flags: Fragment;
GN Name=folB; Synonyms=folQ;
OS Staphylococcus haemolyticus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1283;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8586264; DOI=10.1111/j.1574-6968.1995.tb07932.x;
RA Kellam P., Dallas W.S., Ballantine S.P., Delves C.J.;
RT "Functional cloning of the dihydropteroate synthase gene of Staphylococcus
RT haemolyticus.";
RL FEMS Microbiol. Lett. 134:165-169(1995).
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 -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC43584.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U40768; AAC43584.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q59920; -.
DR SMR; Q59920; -.
DR UniPathway; UPA00077; UER00154.
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..>84
FT /note="Dihydroneopterin aldolase"
FT /id="PRO_0000168286"
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"
FT NON_TER 84
SQ SEQUENCE 84 AA; 9477 MW; 6D3280B6D3EC816B CRC64;
MSDIIFLNGM RFYGYHGALH AENELGQIFI VDVTLKVDLT EAGKTDNVKD TVHYGEVFED
VKNIVEGPSC QLIEHLAERI AKRI
