ID A0A2K4G3Z0_9PSED Unreviewed; 172 AA.
AC A0A2K4G3Z0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:POA18322.1};
GN ORFNames=C1886_17370 {ECO:0000313|EMBL:POA18322.1};
OS Pseudomonas sp. FW300-N1A1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2075555 {ECO:0000313|EMBL:POA18322.1, ECO:0000313|Proteomes:UP000236411};
RN [1] {ECO:0000313|EMBL:POA18322.1, ECO:0000313|Proteomes:UP000236411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW300-N1A1 {ECO:0000313|EMBL:POA18322.1,
RC ECO:0000313|Proteomes:UP000236411};
RA Spencer S.J., Aaring A.B., Hendricks A., Penterman J., Chakraborty R.,
RA Alm E.J.;
RT "Whole genome sequencing of deep branching strains shows evolution and
RT exchange across a contaminated watershed.";
RL Submitted (JAN-2018) 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:POA18322.1}.
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DR EMBL; PPSF01000042; POA18322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K4G3Z0; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000236411; 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:SF2; 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE PYROPHOSPHOKINASE; 1.
DR Pfam; PF01288; HPPK; 1.
DR SUPFAM; SSF55083; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, 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:POA18322.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..130
FT /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT /evidence="ECO:0000259|Pfam:PF01288"
SQ SEQUENCE 172 AA; 18891 MW; 3CBDF075355EB7A4 CRC64;
MSLTQVFLGL GSNVEREAHL RAGLEALSGF LVDIRCSAVF ESQPVGIKSG PFFNFVVSAF
TDLPLMELDR RLKFIEADNG RYAPDRKGLP LDIDVLLYGD LVGNFDGLVL PRAEILKNAF
VLWPLSLIAP DRVHPGVGKS FATLWGEAQI DQVLAPVAFA WRGEQLTPLN LL
//
