ID   FOLX_ECOL6              Reviewed;         120 AA.
AC   P0AC20; P77796; P80449;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 79.
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=c2846;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN81300.1; -; Genomic_DNA.
DR   RefSeq; WP_000068457.1; NC_004431.1.
DR   AlphaFoldDB; P0AC20; -.
DR   SMR; P0AC20; -.
DR   STRING; 199310.c2846; -.
DR   EnsemblBacteria; AAN81300; AAN81300; c2846.
DR   GeneID; 66673814; -.
DR   KEGG; ecc:c2846; -.
DR   eggNOG; COG1539; Bacteria.
DR   HOGENOM; CLU_112632_0_0_6; -.
DR   OMA; DHALNYR; -.
DR   BioCyc; ECOL199310:C2846-MON; -.
DR   Proteomes; UP000001410; 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.
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_0000168297"
SQ   SEQUENCE   120 AA;  14082 MW;  5DDFF76540827ED6 CRC64;
     MAQPAAIIRI KNLRLRTFIG IKEEEINNRQ DIVINVTIHY PADKARTSED INDALNYRTV
     TKNIIQHVEN NRFSLLEKLT QDVLDIAREH HWVTYAEVEI DKLHALRYAD SVSMTLSWQR