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Database: UniProt
Entry: Q0T2I4_SHIF8
LinkDB: Q0T2I4_SHIF8
Original site: Q0T2I4_SHIF8 
ID   Q0T2I4_SHIF8            Unreviewed;       120 AA.
AC   Q0T2I4;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Dihydroneopterin triphosphate 2'-epimerase {ECO:0000256|ARBA:ARBA00044197};
DE            EC=5.1.99.7 {ECO:0000256|ARBA:ARBA00044039};
DE   AltName: Full=D-erythro-7,8-dihydroneopterin triphosphate epimerase {ECO:0000256|ARBA:ARBA00044306};
GN   Name=folX {ECO:0000313|EMBL:ABF04481.1};
GN   OrderedLocusNames=SFV_2370 {ECO:0000313|EMBL:ABF04481.1};
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384 {ECO:0000313|EMBL:ABF04481.1, ECO:0000313|Proteomes:UP000000659};
RN   [1] {ECO:0000313|EMBL:ABF04481.1, ECO:0000313|Proteomes:UP000000659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401 {ECO:0000313|EMBL:ABF04481.1,
RC   ECO:0000313|Proteomes:UP000000659};
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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:0000256|ARBA:ARBA00043806};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|ARBA:ARBA00011823}.
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DR   EMBL; CP000266; ABF04481.1; -; Genomic_DNA.
DR   RefSeq; WP_000068457.1; NC_008258.1.
DR   AlphaFoldDB; Q0T2I4; -.
DR   SMR; Q0T2I4; -.
DR   GeneID; 75205651; -.
DR   KEGG; sfv:SFV_2370; -.
DR   HOGENOM; CLU_112632_0_0_6; -.
DR   Proteomes; UP000000659; Chromosome.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:InterPro.
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   NCBIfam; TIGR00526; folB_dom; 1.
DR   PANTHER; PTHR42844; DIHYDRONEOPTERIN ALDOLASE 1-RELATED; 1.
DR   PANTHER; PTHR42844:SF10; DIHYDRONEOPTERIN TRIPHOSPHATE 2'-EPIMERASE; 1.
DR   Pfam; PF02152; FolB; 1.
DR   SMART; SM00905; FolB; 1.
DR   SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE   4: Predicted;
FT   DOMAIN          8..118
FT                   /note="Dihydroneopterin aldolase/epimerase"
FT                   /evidence="ECO:0000259|SMART:SM00905"
SQ   SEQUENCE   120 AA;  14082 MW;  5DDFF76540827ED6 CRC64;
     MAQPAAIIRI KNLRLRTFIG IKEEEINNRQ DIVINVTIHY PADKARTSED INDALNYRTV
     TKNIIQHVEN NRFSLLEKLT QDVLDIAREH HWVTYAEVEI DKLHALRYAD SVSMTLSWQR
//
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