ID   FOLQ_LACLM              Reviewed;         166 AA.
AC   P0CI35; A2RKW0; Q8GJP2;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Probable DHNTP pyrophosphohydrolase;
DE            EC=3.6.1.-;
DE   AltName: Full=Dihydroneopterin triphosphate pyrophosphohydrolase;
GN   Name=folQ; OrderedLocusNames=llmg_1335;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=12788700; DOI=10.1128/aem.69.6.3069-3076.2003;
RA   Sybesma W., Starrenburg M., Kleerebezem M., Mierau I., de Vos W.M.,
RA   Hugenholtz J.;
RT   "Increased production of folate by metabolic engineering of Lactococcus
RT   lactis.";
RL   Appl. Environ. Microbiol. 69:3069-3076(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
CC   -!- FUNCTION: Probably mediates the removal of pyrophosphate from
CC       dihydroneopterin triphosphate (DHNTP), a possible step in the pterin
CC       branch of the folate synthesis pathway. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC       4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC       dihydroneopterin triphosphate: step 1/4.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR   EMBL; AY156932; AAN64308.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL97926.1; -; Genomic_DNA.
DR   RefSeq; WP_011835208.1; NZ_WJVF01000034.1.
DR   AlphaFoldDB; P0CI35; -.
DR   SMR; P0CI35; -.
DR   STRING; 416870.llmg_1335; -.
DR   EnsemblBacteria; CAL97926; CAL97926; llmg_1335.
DR   KEGG; llm:llmg_1335; -.
DR   eggNOG; COG1051; Bacteria.
DR   HOGENOM; CLU_131409_0_0_9; -.
DR   OMA; FIRHPYL; -.
DR   BioCyc; LLAC416870:LLMG_RS06765-MON; -.
DR   UniPathway; UPA00077; UER00152.
DR   Proteomes; UP000000364; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW   One-carbon metabolism.
FT   CHAIN           1..166
FT                   /note="Probable DHNTP pyrophosphohydrolase"
FT                   /id="PRO_0000057132"
FT   DOMAIN          42..166
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           73..94
FT                   /note="Nudix box"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   166 AA;  19612 MW;  5B2857EB08DB3353 CRC64;
     MNEDLISQIK EVVTAENQEK LIKIIQLLES SNYELRGKIN PDLQLSASAL VFKEDKLFFI
     EHPYQKELLL PAGHVELKES PLDTAIREFH EETGFFAKKM GKLVDVNLID IPFNETKNEK
     KHQHIDFRYL LELEEQEAEL AELPFFLLEL EEAPEEFKKY YRYKNI