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Database: UniProt
Entry: A0A1Q9LCL5_9PSEU
LinkDB: A0A1Q9LCL5_9PSEU
Original site: A0A1Q9LCL5_9PSEU 
ID   A0A1Q9LCL5_9PSEU        Unreviewed;       161 AA.
AC   A0A1Q9LCL5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase {ECO:0000256|ARBA:ARBA00013253};
DE            EC=2.7.6.3 {ECO:0000256|ARBA:ARBA00013253};
GN   ORFNames=BJP25_01615 {ECO:0000313|EMBL:OLR89754.1};
OS   Actinokineospora bangkokensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=1193682 {ECO:0000313|EMBL:OLR89754.1, ECO:0000313|Proteomes:UP000186040};
RN   [1] {ECO:0000313|EMBL:OLR89754.1, ECO:0000313|Proteomes:UP000186040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44EHW {ECO:0000313|EMBL:OLR89754.1,
RC   ECO:0000313|Proteomes:UP000186040};
RA   Greule A., Intra B., Flemming S., Rommel M.G., Panbangred W., Bechthold A.;
RT   "The Draft Genome Sequence of Actinokineospora bangkokensis 44EHWT reveals
RT   the biosynthetic pathway of antifungal compounds Thailandins with unusual
RT   extender unit butylmalonyl-CoA.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:OLR89754.1}.
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DR   EMBL; MKQR01000028; OLR89754.1; -; Genomic_DNA.
DR   RefSeq; WP_075977964.1; NZ_MKQR01000028.1.
DR   AlphaFoldDB; A0A1Q9LCL5; -.
DR   STRING; 1193682.BJP25_01615; -.
DR   OrthoDB; 9808041at2; -.
DR   UniPathway; UPA00077; UER00155.
DR   Proteomes; UP000186040; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OLR89754.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186040};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          85..96
FT                   /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT                   /evidence="ECO:0000259|PROSITE:PS00794"
SQ   SEQUENCE   161 AA;  17219 MW;  7AF8DADBB534649C CRC64;
     MSRAVLSLGS NLGDRLAHLR SAVTAFADEL VAVSPVYETA AWGVTDQPDF LNAVVVVAAD
     GVDGWGWLRR GQAAEDAAGR VRERRWGPRT LDVDVVTVDG VTSDHPELLL PHPGTAERAT
     VLVPWLDVEP DAVVPGVGPA RDLLAGLDTS GVRRRDDLEL R
//
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