ID   Q0I4C1_HISS1            Unreviewed;       158 AA.
AC   Q0I4C1;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
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:ABI25300.1};
GN   OrderedLocusNames=HS_1025 {ECO:0000313|EMBL:ABI25300.1};
OS   Histophilus somni (strain 129Pt) (Haemophilus somnus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914 {ECO:0000313|EMBL:ABI25300.1};
RN   [1] {ECO:0000313|EMBL:ABI25300.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129PT {ECO:0000313|EMBL:ABI25300.1};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Dalin E., Tice H., Pitluck S., Brettin T.S., Bruce D., Challacombe J.F.,
RA   Chertkov O., Detter J.C., Gilna P., Han S., Misra M., Tapia R.,
RA   Thayer N.N., Xie G., Inzana T.J., Duncan A.J., Siddaramppa S.,
RA   Richardson P.;
RT   "Complete genome sequence of Haemophilus somnus 129PT.";
RL   Submitted (AUG-2006) 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}.
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DR   EMBL; CP000436; ABI25300.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0I4C1; -.
DR   KEGG; hso:HS_1025; -.
DR   eggNOG; COG0801; Bacteria.
DR   HOGENOM; CLU_097916_2_3_6; -.
DR   UniPathway; UPA00077; UER00155.
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:ABI25300.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABI25300.1}.
FT   DOMAIN          88..99
FT                   /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT                   /evidence="ECO:0000259|PROSITE:PS00794"
SQ   SEQUENCE   158 AA;  18082 MW;  46D9A63E05A3750A CRC64;
     MKTVYIALGS NLDTPIQQLN LALGSLAQLK SCKLSAVSSF YQSKPLGPQD QPDYVNAVAC
     LKTELDPIAL LDQLQHIENQ QGRVRLRRWG ERTLDLDILL YGNEIIQNER LTIPHYDMKN
     REFVIIPLYE IAPHLILPHG EKLADIMLNF THHKMQKL
//