FOLX_ECO57
ID FOLX_ECO57 Reviewed; 120 AA.
AC P0AC21; P77796; P80449;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 93.
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=Z3565, ECs3187;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG57432.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36610.1; -; Genomic_DNA.
DR PIR; C91027; C91027.
DR PIR; D85871; D85871.
DR RefSeq; NP_311214.1; NC_002695.1.
DR RefSeq; WP_000068457.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AC21; -.
DR SMR; P0AC21; -.
DR STRING; 155864.EDL933_3468; -.
DR EnsemblBacteria; AAG57432; AAG57432; Z3565.
DR EnsemblBacteria; BAB36610; BAB36610; ECs_3187.
DR GeneID; 66673814; -.
DR GeneID; 916895; -.
DR KEGG; ece:Z3565; -.
DR KEGG; ecs:ECs_3187; -.
DR PATRIC; fig|386585.9.peg.3327; -.
DR eggNOG; COG1539; Bacteria.
DR HOGENOM; CLU_112632_0_0_6; -.
DR OMA; DHALNYR; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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_0000168296"
SQ SEQUENCE 120 AA; 14082 MW; 5DDFF76540827ED6 CRC64;
MAQPAAIIRI KNLRLRTFIG IKEEEINNRQ DIVINVTIHY PADKARTSED INDALNYRTV
TKNIIQHVEN NRFSLLEKLT QDVLDIAREH HWVTYAEVEI DKLHALRYAD SVSMTLSWQR