FOLQ_LACLA
ID FOLQ_LACLA Reviewed; 165 AA.
AC Q9CGE1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable DHNTP pyrophosphohydrolase;
DE EC=3.6.1.-;
DE AltName: Full=Dihydroneopterin triphosphate pyrophosphohydrolase;
GN Name=folQ; OrderedLocusNames=LL1156; ORFNames=L168057;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005176; AAK05254.1; -; Genomic_DNA.
DR PIR; D86769; D86769.
DR RefSeq; NP_267312.1; NC_002662.1.
DR RefSeq; WP_003132112.1; NC_002662.1.
DR AlphaFoldDB; Q9CGE1; -.
DR SMR; Q9CGE1; -.
DR STRING; 272623.L168057; -.
DR PaxDb; Q9CGE1; -.
DR EnsemblBacteria; AAK05254; AAK05254; L168057.
DR KEGG; lla:L168057; -.
DR PATRIC; fig|272623.7.peg.1236; -.
DR eggNOG; COG1051; Bacteria.
DR HOGENOM; CLU_131409_0_0_9; -.
DR OMA; FIRHPYL; -.
DR BioCyc; MetaCyc:MON-13396; -.
DR UniPathway; UPA00077; UER00152.
DR Proteomes; UP000002196; 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; Reference proteome.
FT CHAIN 1..165
FT /note="Probable DHNTP pyrophosphohydrolase"
FT /id="PRO_0000057131"
FT DOMAIN 42..165
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 165 AA; 19157 MW; 1A0A8D71B911728D CRC64;
MNEDLIAEIQ ALSAIGSEEK FSEIIRLLKN STLELRGKKN PDLQLSASAL VFKKHKLFFI
EHPYQKELLL PAGHVELGEK PLETAIREFH EETGFSASES GKLVDVNLIN IPYNKIKNEK
EHQHIDFRFL LELKEKEAGL AELPFFLLDR TEAPDEFKKY YQYKR
