ID   FOLQ_LACLN              Reviewed;         166 AA.
AC   D8KIT5; A2RKW0; Q8GJP2;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Probable DHNTP pyrophosphohydrolase;
DE            EC=3.6.1.-;
DE   AltName: Full=Dihydroneopterin triphosphate pyrophosphohydrolase;
GN   Name=folQ; OrderedLocusNames=LLNZ_06905;
OS   Lactococcus lactis subsp. cremoris (strain NZ9000).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=746361;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZ9000;
RX   PubMed=20639323; DOI=10.1128/jb.00533-10;
RA   Linares D.M., Kok J., Poolman B.;
RT   "Genome sequences of Lactococcus lactis MG1363 (revised) and NZ9000 and
RT   comparative physiological studies.";
RL   J. Bacteriol. 192:5806-5812(2010).
RN   [2]
RP   FUNCTION, ENZYME ACTIVITY, SUBUNIT, COFACTOR, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=NZ9000;
RX   PubMed=15611104; DOI=10.1074/jbc.m413759200;
RA   Klaus S.M.J., Wegkamp A., Sybesma W., Hugenholtz J., Gregory J.F. III,
RA   Hanson A.D.;
RT   "A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in
RT   the folate synthesis pathway of bacteria and plants.";
RL   J. Biol. Chem. 280:5274-5280(2005).
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:0000269|PubMed:15611104}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:15611104};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.1 uM for DHNTP {ECO:0000269|PubMed:15611104};
CC         Vmax=0.65 umol/min/mg enzyme with DHNTP as substrate
CC         {ECO:0000269|PubMed:15611104};
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:0000269|PubMed:15611104}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR   EMBL; CP002094; ADJ60331.1; -; Genomic_DNA.
DR   RefSeq; WP_011835208.1; NC_017949.1.
DR   AlphaFoldDB; D8KIT5; -.
DR   SMR; D8KIT5; -.
DR   KEGG; lln:LLNZ_06905; -.
DR   PATRIC; fig|746361.3.peg.1388; -.
DR   HOGENOM; CLU_131409_0_0_9; -.
DR   OMA; FIRHPYL; -.
DR   OrthoDB; 1308416at2; -.
DR   BioCyc; LLAC746361:LLNZ_RS06770-MON; -.
DR   BRENDA; 3.6.1.67; 2903.
DR   UniPathway; UPA00077; UER00152.
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   1: Evidence at protein level;
KW   Folate biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW   One-carbon metabolism.
FT   CHAIN           1..166
FT                   /note="Probable DHNTP pyrophosphohydrolase"
FT                   /id="PRO_0000402186"
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