FOLB_SHIFL
ID FOLB_SHIFL Reviewed; 122 AA.
AC P0AC18; P31055; P76659;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=SF3099, S3304;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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:0000250|UniProtKB:P0AC16}.
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:P0AC16};
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000305}.
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DR EMBL; AE005674; AAN44575.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP18387.1; -; Genomic_DNA.
DR RefSeq; NP_708868.2; NC_004337.2.
DR RefSeq; WP_001295541.1; NZ_WPGW01000061.1.
DR AlphaFoldDB; P0AC18; -.
DR SMR; P0AC18; -.
DR STRING; 198214.SF3099; -.
DR EnsemblBacteria; AAN44575; AAN44575; SF3099.
DR EnsemblBacteria; AAP18387; AAP18387; S3304.
DR GeneID; 1026693; -.
DR GeneID; 67414995; -.
DR KEGG; sfl:SF3099; -.
DR KEGG; sfx:S3304; -.
DR PATRIC; fig|198214.7.peg.3677; -.
DR HOGENOM; CLU_112632_0_2_6; -.
DR OMA; GIYEWEK; -.
DR OrthoDB; 1858654at2; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 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; Reference proteome.
FT CHAIN 1..122
FT /note="Dihydroneopterin aldolase"
FT /id="PRO_0000168271"
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 122 AA; 13620 MW; BEA82C1E0AA38A55 CRC64;
MDIVFIEQLS VITTIGVYDW EQTIEQKLVF DIEMAWDNRK AAKSDDVADC LSYADIAETV
VSHVEGARFA LVERVAEEVA ELLLARFNSP WVRIKLSKPG AVARAANVGV IIERGNNLKE
NN
