FOLB_STAAU
ID FOLB_STAAU Reviewed; 121 AA.
AC P56740;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Dihydroneopterin aldolase {ECO:0000303|PubMed:9586996};
DE Short=DHNA {ECO:0000303|PubMed:9586996};
DE EC=4.1.2.25 {ECO:0000269|PubMed:9586996};
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;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP 6-HYDROXYMETHYL-7,8-DIHYDRONEOPTERIN, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, ACTIVE SITE, AND
RP SUBUNIT.
RC STRAIN=ATCC 25923 / DSM 1104 / JCM 2413 / NBRC 14462 / NCIMB 12702 / NCTC
RC 12981 / Seattle 1945;
RX PubMed=9586996; DOI=10.1038/nsb0598-357;
RA Hennig M., D'Arcy A., Hampele I.C., Page M.G., Oefner C., Dale G.E.;
RT "Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase
RT from Staphylococcus aureus.";
RL Nat. Struct. Biol. 5:357-362(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH
RP 7,8-DIHYDRONEOPTERIN ANALOGS.
RX PubMed=15027862; DOI=10.1021/jm030497y;
RA Sanders W.J., Nienaber V.L., Lerner C.G., McCall J.O., Merrick S.M.,
RA Swanson S.J., Harlan J.E., Stoll V.S., Stamper G.F., Betz S.F.,
RA Condroski K.R., Meadows R.P., Severin J.M., Walter K.A., Magdalinos P.,
RA Jakob C.G., Wagner R., Beutel B.A.;
RT "Discovery of potent inhibitors of dihydroneopterin aldolase using
RT CrystaLEAD high-throughput X-ray crystallographic screening and structure-
RT directed lead optimization.";
RL J. Med. Chem. 47:1709-1718(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEXES WITH D-MONAPTERIN AND
RP L-NEOPTERIN, FUNCTION, REACTION MECHANISM, AND ACTIVE SITE.
RX PubMed=17331536; DOI=10.1016/j.jmb.2007.02.009;
RA Blaszczyk J., Li Y., Gan J., Yan H., Ji X.;
RT "Structural basis for the aldolase and epimerase activities of
RT Staphylococcus aureus dihydroneopterin aldolase.";
RL J. Mol. Biol. 368:161-169(2007).
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:0000269|PubMed:17331536, ECO:0000269|PubMed:9586996}.
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:0000269|PubMed:9586996};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:9586996};
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. {ECO:0000269|PubMed:9586996}.
CC -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000305}.
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DR RefSeq; WP_001154303.1; NZ_WKIW01000023.1.
DR PDB; 1DHN; X-ray; 1.65 A; A=1-121.
DR PDB; 1RRI; X-ray; 2.00 A; A=1-121.
DR PDB; 1RRW; X-ray; 2.21 A; A=1-121.
DR PDB; 1RRY; X-ray; 2.70 A; A=1-121.
DR PDB; 1RS2; X-ray; 2.31 A; A=1-121.
DR PDB; 1RS4; X-ray; 2.70 A; A=1-121.
DR PDB; 1RSD; X-ray; 2.50 A; A=1-121.
DR PDB; 1RSI; X-ray; 2.20 A; A=1-121.
DR PDB; 1U68; X-ray; 2.40 A; A=1-121.
DR PDB; 2DHN; X-ray; 2.20 A; A=1-121.
DR PDB; 2NM2; X-ray; 1.70 A; A/B/C/D=1-121.
DR PDB; 2NM3; X-ray; 1.68 A; A=1-121.
DR PDBsum; 1DHN; -.
DR PDBsum; 1RRI; -.
DR PDBsum; 1RRW; -.
DR PDBsum; 1RRY; -.
DR PDBsum; 1RS2; -.
DR PDBsum; 1RS4; -.
DR PDBsum; 1RSD; -.
DR PDBsum; 1RSI; -.
DR PDBsum; 1U68; -.
DR PDBsum; 2DHN; -.
DR PDBsum; 2NM2; -.
DR PDBsum; 2NM3; -.
DR AlphaFoldDB; P56740; -.
DR BMRB; P56740; -.
DR SMR; P56740; -.
DR ChEMBL; CHEMBL3217378; -.
DR DrugBank; DB01906; 3-(5-amino-7-hydroxy-(1,2,3)triazolo(4,5-d)pyrimidin-2-yl)benzoic acid.
DR DrugBank; DB03571; 3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(3,5-dichlorobenzyl)-benzamide.
DR DrugBank; DB03231; 3-(5-Amino-7-oxo-3,7-dihydro-2H-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(2-{[2-(hydroxymethyl)phenyl]sulfanyl}benzyl)benzamide.
DR DrugBank; DB02119; 6-Hydroxymethyl-7,8-Dihydropterin.
DR DrugBank; DB04425; 7,8-Dihydroneopterin.
DR DrugBank; DB01778; 8-Aminotheophylline.
DR DrugBank; DB02489; 9-Methylguanine.
DR DrugBank; DB04168; Bropirimine.
DR DrugBank; DB06906; ethyl 2-amino-4-hydroxypyrimidine-5-carboxylate.
DR DrugBank; DB04400; L-erythro-7,8-dihydrobiopterin.
DR OMA; GHYKSVA; -.
DR BRENDA; 4.1.2.25; 3352.
DR BRENDA; 5.1.99.8; 3352.
DR UniPathway; UPA00077; UER00154.
DR EvolutionaryTrace; P56740; -.
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 1: Evidence at protein level;
KW 3D-structure; Folate biosynthesis; Isomerase; Lyase.
FT CHAIN 1..121
FT /note="Dihydroneopterin aldolase"
FT /id="PRO_0000168283"
FT ACT_SITE 100
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:17331536,
FT ECO:0000305|PubMed:9586996"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:17331536,
FT ECO:0000305|PubMed:9586996, ECO:0007744|PDB:2NM2"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:17331536,
FT ECO:0000305|PubMed:9586996, ECO:0007744|PDB:2NM2"
FT BINDING 73..74
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:17331536,
FT ECO:0000305|PubMed:9586996, ECO:0007744|PDB:2NM2"
FT STRAND 4..14
FT /evidence="ECO:0007829|PDB:1DHN"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1DHN"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:1DHN"
FT STRAND 27..37
FT /evidence="ECO:0007829|PDB:1DHN"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:1DHN"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1DHN"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:1DHN"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2NM2"
FT HELIX 73..87
FT /evidence="ECO:0007829|PDB:1DHN"
FT STRAND 91..102
FT /evidence="ECO:0007829|PDB:1DHN"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:1DHN"
SQ SEQUENCE 121 AA; 13751 MW; 55B267FB69CA3D8D CRC64;
MQDTIFLKGM RFYGYHGALS AENEIGQIFK VDVTLKVDLS EAGRTDNVID TVHYGEVFEE
VKSIMEGKAV NLLEHLAERI ANRINSQYNR VMETKVRITK ENPPIPGHYD GVGIEIVREN
K
