ID A0A2N4UK55_9BURK Unreviewed; 161 AA.
AC A0A2N4UK55;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase {ECO:0000256|ARBA:ARBA00016218};
DE EC=2.7.6.3 {ECO:0000256|ARBA:ARBA00013253};
DE AltName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000256|ARBA:ARBA00029766};
DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase {ECO:0000256|ARBA:ARBA00033413};
GN Name=folK {ECO:0000313|EMBL:PLC55390.1};
GN ORFNames=CR155_04105 {ECO:0000313|EMBL:PLC55390.1};
OS Pollutimonas nitritireducens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pollutimonas.
OX NCBI_TaxID=2045209 {ECO:0000313|EMBL:PLC55390.1, ECO:0000313|Proteomes:UP000234328};
RN [1] {ECO:0000313|EMBL:PLC55390.1, ECO:0000313|Proteomes:UP000234328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JR1/69-2-13 {ECO:0000313|EMBL:PLC55390.1,
RC ECO:0000313|Proteomes:UP000234328};
RA Grouzdev D.S., Tourova T.P., Goeva M.A., Babich T.L., Sokolova D.S.,
RA Abdullin R., Poltaraus A.B., Toshchakov S.V., Nazina T.N.;
RT "Two draft genome sequences of Pusillimonas sp. strains isolated from a
RT nitrate- and radionuclide-contaminated groundwater in Russia.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of pyrophosphate from adenosine
CC triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic
CC step in folate biosynthesis pathway. {ECO:0000256|ARBA:ARBA00029409}.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 4/4.
CC {ECO:0000256|ARBA:ARBA00005051}.
CC -!- SIMILARITY: Belongs to the HPPK family.
CC {ECO:0000256|ARBA:ARBA00005810}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLC55390.1}.
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DR EMBL; PDNV01000002; PLC55390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4UK55; -.
DR OrthoDB; 9808041at2; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000234328; Unassembled WGS sequence.
DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00483; HPPK; 1.
DR Gene3D; 3.30.70.560; 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK; 1.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR NCBIfam; TIGR01498; folK; 1.
DR PANTHER; PTHR43071; 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE PYROPHOSPHOKINASE; 1.
DR PANTHER; PTHR43071:SF1; 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE PYROPHOSPHOKINASE; 1.
DR Pfam; PF01288; HPPK; 1.
DR SUPFAM; SSF55083; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK; 1.
DR PROSITE; PS00794; HPPK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PLC55390.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000234328};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 90..101
FT /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT /evidence="ECO:0000259|PROSITE:PS00794"
SQ SEQUENCE 161 AA; 17664 MW; 2D8522BE570BA7CC CRC64;
MHDDATVFIG LGANLGDART CIEQATAQLA AWPGIDDFVL SPLYRSAPVD SSGPDYVNAV
AQFATRLSAR DVLRILQGLE LAHGRLRPYR NAPRTLDLDL LLYGTQDIRE PDLIVPHPRM
HERAFVLRPL ADLAPTLRLA QGPIATLLAD CSYQELSPLP D
//
