ID   FOLX_SHIFL              Reviewed;         120 AA.
AC   P0AC22; P77796; P80449;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Dihydroneopterin triphosphate 2'-epimerase;
DE            EC=5.1.99.7 {ECO:0000250|UniProtKB:P0AC19};
DE   AltName: Full=D-erythro-7,8-dihydroneopterin triphosphate epimerase;
GN   Name=folX; OrderedLocusNames=SF2379, S2514;
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 epimerization of carbon 2' of the side chain of
CC       7,8-dihydroneopterin triphosphate (H2NTP) to form 7,8-dihydromonapterin
CC       triphosphate (H2MTP). Is required for tetrahydromonapterin
CC       biosynthesis. {ECO:0000250|UniProtKB:P0AC19}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin
CC         3'-triphosphate; Xref=Rhea:RHEA:28346, ChEBI:CHEBI:58462,
CC         ChEBI:CHEBI:61186; EC=5.1.99.7;
CC         Evidence={ECO:0000250|UniProtKB:P0AC19};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250|UniProtKB:P0AC19}.
CC   -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN43892.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17710.1; -; Genomic_DNA.
DR   RefSeq; NP_708185.1; NC_004337.2.
DR   RefSeq; WP_000068457.1; NZ_WPGW01000016.1.
DR   AlphaFoldDB; P0AC22; -.
DR   SMR; P0AC22; -.
DR   STRING; 198214.SF2379; -.
DR   EnsemblBacteria; AAN43892; AAN43892; SF2379.
DR   EnsemblBacteria; AAP17710; AAP17710; S2514.
DR   GeneID; 1027228; -.
DR   GeneID; 66673814; -.
DR   KEGG; sfl:SF2379; -.
DR   KEGG; sfx:S2514; -.
DR   PATRIC; fig|198214.7.peg.2846; -.
DR   HOGENOM; CLU_112632_0_0_6; -.
DR   OMA; DHALNYR; -.
DR   OrthoDB; 1858654at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:InterPro.
DR   GO; GO:0008719; F:dihydroneopterin triphosphate 2'-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006760; P:folic acid-containing compound metabolic process; IEA:InterPro.
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; TIGR00526; folB_dom; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC19"
FT   CHAIN           2..120
FT                   /note="Dihydroneopterin triphosphate 2'-epimerase"
FT                   /id="PRO_0000168298"
SQ   SEQUENCE   120 AA;  14082 MW;  5DDFF76540827ED6 CRC64;
     MAQPAAIIRI KNLRLRTFIG IKEEEINNRQ DIVINVTIHY PADKARTSED INDALNYRTV
     TKNIIQHVEN NRFSLLEKLT QDVLDIAREH HWVTYAEVEI DKLHALRYAD SVSMTLSWQR