FOLB_ECOLI
ID FOLB_ECOLI Reviewed; 122 AA.
AC P0AC16; P31055; P76659; Q2M9E7;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Dihydroneopterin aldolase {ECO:0000303|PubMed:9651328};
DE Short=DHNA {ECO:0000303|PubMed:25264482};
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 {ECO:0000303|PubMed:9651328}; Synonyms=ygiG;
GN OrderedLocusNames=b3058, JW3030;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / ATCC 35607 / JM83;
RX PubMed=8389741; DOI=10.1128/jb.175.12.3784-3789.1993;
RA Cain B.D., Norton P.J., Eubanks W., Nick H.S., Allen C.M.;
RT "Amplification of the bacA gene confers bacitracin resistance to
RT Escherichia coli.";
RL J. Bacteriol. 175:3784-3789(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP REACTION 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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS) IN COMPLEX WITH L-NEOPTERIN, AND
RP REACTION MECHANISM.
RX PubMed=25264482; DOI=10.1186/2045-3701-4-52;
RA Blaszczyk J., Lu Z., Li Y., Yan H., Ji X.;
RT "Crystallographic and molecular dynamics simulation analysis of Escherichia
RT coli dihydroneopterin aldolase.";
RL Cell Biosci. 4:52-52(2014).
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 at appreciable
CC velocity. {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=64 uM for 7,8-dihydroneopterin in aldolase reaction
CC {ECO:0000269|PubMed:9651328};
CC KM=45 uM for 7,8-dihydroneopterin in epimerase reaction
CC {ECO:0000269|PubMed:9651328};
CC KM=36 uM for 7,8-dihydromonapterin in aldolase reaction
CC {ECO:0000269|PubMed:9651328};
CC KM=57 uM for 7,8-dihydromonapterin in epimerase reaction
CC {ECO:0000269|PubMed:9651328};
CC Vmax=127 umol/h/mg enzyme toward 7,8-dihydroneopterin in aldolase
CC reaction {ECO:0000269|PubMed:9651328};
CC Vmax=20.3 umol/h/mg enzyme toward 7,8-dihydroneopterin in epimerase
CC reaction {ECO:0000269|PubMed:9651328};
CC Vmax=158 umol/h/mg enzyme toward 7,8-dihydromonapterin in aldolase
CC reaction {ECO:0000269|PubMed:9651328};
CC Vmax=15.6 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 -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:9651328}.
CC -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA89138.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L12966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U28379; AAA89138.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76094.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77109.1; -; Genomic_DNA.
DR PIR; H65093; H65093.
DR RefSeq; NP_417530.2; NC_000913.3.
DR RefSeq; WP_001295541.1; NZ_STEB01000001.1.
DR PDB; 2O90; X-ray; 1.07 A; A=1-122.
DR PDBsum; 2O90; -.
DR AlphaFoldDB; P0AC16; -.
DR SMR; P0AC16; -.
DR DIP; DIP-36044N; -.
DR IntAct; P0AC16; 2.
DR STRING; 511145.b3058; -.
DR PaxDb; P0AC16; -.
DR PRIDE; P0AC16; -.
DR EnsemblBacteria; AAC76094; AAC76094; b3058.
DR EnsemblBacteria; BAE77109; BAE77109; BAE77109.
DR GeneID; 67414995; -.
DR GeneID; 947544; -.
DR KEGG; ecj:JW3030; -.
DR KEGG; eco:b3058; -.
DR PATRIC; fig|1411691.4.peg.3673; -.
DR EchoBASE; EB1624; -.
DR eggNOG; COG1539; Bacteria.
DR HOGENOM; CLU_112632_0_2_6; -.
DR InParanoid; P0AC16; -.
DR OMA; GIYEWEK; -.
DR PhylomeDB; P0AC16; -.
DR BioCyc; EcoCyc:H2NEOPTERINALDOL-MON; -.
DR BioCyc; MetaCyc:H2NEOPTERINALDOL-MON; -.
DR BRENDA; 1.13.11.81; 2026.
DR BRENDA; 4.1.2.25; 2026.
DR SABIO-RK; P0AC16; -.
DR UniPathway; UPA00077; UER00154.
DR EvolutionaryTrace; P0AC16; -.
DR PRO; PR:P0AC16; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
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; Reference proteome.
FT CHAIN 1..122
FT /note="Dihydroneopterin aldolase"
FT /id="PRO_0000168269"
FT ACT_SITE 98
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P56740,
FT ECO:0000305|PubMed:25264482"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:25264482,
FT ECO:0007744|PDB:2O90"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:25264482,
FT ECO:0007744|PDB:2O90"
FT BINDING 72..73
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:25264482,
FT ECO:0007744|PDB:2O90"
FT CONFLICT 81..82
FT /note="EL -> DV (in Ref. 1; L12966)"
FT /evidence="ECO:0000305"
FT CONFLICT 100..122
FT /note="GAVARAANVGVIIERGNNLKENN -> ASGAGGECWRNH (in Ref. 1;
FT L12966)"
FT /evidence="ECO:0000305"
FT STRAND 2..15
FT /evidence="ECO:0007829|PDB:2O90"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:2O90"
FT STRAND 26..36
FT /evidence="ECO:0007829|PDB:2O90"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:2O90"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:2O90"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:2O90"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2O90"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:2O90"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:2O90"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:2O90"
SQ SEQUENCE 122 AA; 13620 MW; BEA82C1E0AA38A55 CRC64;
MDIVFIEQLS VITTIGVYDW EQTIEQKLVF DIEMAWDNRK AAKSDDVADC LSYADIAETV
VSHVEGARFA LVERVAEEVA ELLLARFNSP WVRIKLSKPG AVARAANVGV IIERGNNLKE
NN
