FOLB_HAEIN
ID FOLB_HAEIN Reviewed; 118 AA.
AC P46362;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Dihydroneopterin aldolase {ECO:0000303|PubMed:9651328};
DE Short=DHNA;
DE EC=4.1.2.25 {ECO:0000269|PubMed:9651328};
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:0000269|PubMed:9651328};
DE AltName: Full=Dihydroneopterin epimerase;
GN Name=folB; OrderedLocusNames=HI_0265;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION
RP MECHANISM.
RX PubMed=9651328; DOI=10.1074/jbc.273.28.17418;
RA Haussmann C., Rohdich F., Schmidt E., Bacher A., Richter G.;
RT "Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic
RT similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin
RT aldolase.";
RL J. Biol. Chem. 273:17418-17424(1998).
CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC hydroxymethyl-7,8-dihydropterin. Can use L-threo-dihydroneopterin and
CC D-erythro-dihydroneopterin as substrates for the formation of 6-
CC hydroxymethyldihydropterin, but it can also catalyze the epimerization
CC of carbon 2' of dihydroneopterin to dihydromonapterin.
CC {ECO:0000269|PubMed:9651328}.
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:9651328};
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:0000269|PubMed:9651328};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for 7,8-dihydroneopterin in aldolase reaction
CC {ECO:0000269|PubMed:9651328};
CC KM=43 uM for 7,8-dihydroneopterin in epimerase reaction
CC {ECO:0000269|PubMed:9651328};
CC KM=16 uM for 7,8-dihydromonapterin in aldolase reaction
CC {ECO:0000269|PubMed:9651328};
CC KM=19 uM for 7,8-dihydromonapterin in epimerase reaction
CC {ECO:0000269|PubMed:9651328};
CC Vmax=242 umol/h/mg enzyme toward 7,8-dihydroneopterin in aldolase
CC reaction {ECO:0000269|PubMed:9651328};
CC Vmax=1.67 umol/h/mg enzyme toward 7,8-dihydroneopterin in epimerase
CC reaction {ECO:0000269|PubMed:9651328};
CC Vmax=9.9 umol/h/mg enzyme toward 7,8-dihydromonapterin in aldolase
CC reaction {ECO:0000269|PubMed:9651328};
CC Vmax=1.43 umol/h/mg enzyme toward 7,8-dihydromonapterin in epimerase
CC reaction {ECO:0000269|PubMed:9651328};
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 ---------------------------------------------------------------------------
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; L42023; AAC21930.1; -; Genomic_DNA.
DR RefSeq; NP_438434.1; NC_000907.1.
DR RefSeq; WP_005656206.1; NC_000907.1.
DR AlphaFoldDB; P46362; -.
DR SMR; P46362; -.
DR STRING; 71421.HI_0265; -.
DR EnsemblBacteria; AAC21930; AAC21930; HI_0265.
DR KEGG; hin:HI_0265; -.
DR PATRIC; fig|71421.8.peg.280; -.
DR eggNOG; COG1539; Bacteria.
DR HOGENOM; CLU_112632_0_2_6; -.
DR OMA; GIYEWEK; -.
DR PhylomeDB; P46362; -.
DR BioCyc; HINF71421:G1GJ1-280-MON; -.
DR SABIO-RK; P46362; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IBA:GO_Central.
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 Folate biosynthesis; Isomerase; Lyase; Reference proteome.
FT CHAIN 1..118
FT /note="Dihydroneopterin aldolase"
FT /id="PRO_0000168272"
FT ACT_SITE 98
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 72..73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
SQ SEQUENCE 118 AA; 13577 MW; 158C716C473DC701 CRC64;
MDRVFIEELT VFAQIGVYDW EQQIKQKLVF DLEMAWDCKQ AAETDDVVYC LNYAEVSQAI
IDYVESKPFL LIERVAYEVA DLLESRYQLQ GLKIKLSKPK AVAQARNVGV LIVRGCLK
