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Database: UniProt
Entry: A0A2P8KR52_9BURK
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ID   A0A2P8KR52_9BURK        Unreviewed;       186 AA.
AC   A0A2P8KR52;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
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:PSL85410.1};
GN   ORFNames=C7T35_06810 {ECO:0000313|EMBL:PSL85410.1}, GXN78_06230
GN   {ECO:0000313|EMBL:NDZ12473.1};
OS   Variovorax sp. WS11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1105204 {ECO:0000313|EMBL:PSL85410.1, ECO:0000313|Proteomes:UP000241151};
RN   [1] {ECO:0000313|EMBL:PSL85410.1, ECO:0000313|Proteomes:UP000241151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WS11 {ECO:0000313|EMBL:PSL85410.1,
RC   ECO:0000313|Proteomes:UP000241151};
RA   Crombie A.T., Mejia-Florez N.L., Murrell C.;
RT   "Isoprene degraders from the Poplar phyllosphere.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:NDZ12473.1, ECO:0000313|Proteomes:UP000479786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WS11 {ECO:0000313|EMBL:NDZ12473.1,
RC   ECO:0000313|Proteomes:UP000479786};
RA   Dawson R.A., Larke-Mejia N.L., Crombie A.T., Ul-Haque M.F., Murrell J.C.;
RT   "Isoprene oxidation by the Gram negative model bacterium Variovorax sp.
RT   WS11.";
RL   Submitted (FEB-2020) 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:PSL85410.1}.
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DR   EMBL; JAAGOW010000001; NDZ12473.1; -; Genomic_DNA.
DR   EMBL; PXZZ01000007; PSL85410.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8KR52; -.
DR   OrthoDB; 9808041at2; -.
DR   UniPathway; UPA00077; UER00155.
DR   Proteomes; UP000241151; Unassembled WGS sequence.
DR   Proteomes; UP000479786; 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:PSL85410.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:NDZ12473.1}.
FT   DOMAIN          122..133
FT                   /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT                   /evidence="ECO:0000259|PROSITE:PS00794"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   186 AA;  19843 MW;  ED4FC4CA556C2653 CRC64;
     MASSPPPRRA SAAAGVSRAP AARPAAASRP NDVSTDTPAY VAIGANLGDA QATVRRAMDD
     LAALPLTRLT ARSSLYRSAP FEAQGPDFIN AVVELRTSLD PLALLAELQR LEAEAGRERP
     YRNAPRTLDL DLLRHGDATM QSAVLTLPHP RIGERAFVLL PLAEIAPTLV TAAQLERVAG
     QRIERL
//
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