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Database: UniProt
Entry: A0A2V3W6T5_9PROT
LinkDB: A0A2V3W6T5_9PROT
Original site: A0A2V3W6T5_9PROT 
ID   A0A2V3W6T5_9PROT        Unreviewed;       165 AA.
AC   A0A2V3W6T5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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   ORFNames=C8R34_10642 {ECO:0000313|EMBL:PXW88894.1};
OS   Nitrosomonas sp. Nm84.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=200124 {ECO:0000313|EMBL:PXW88894.1, ECO:0000313|Proteomes:UP000248024};
RN   [1] {ECO:0000313|EMBL:PXW88894.1, ECO:0000313|Proteomes:UP000248024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm84 {ECO:0000313|EMBL:PXW88894.1,
RC   ECO:0000313|Proteomes:UP000248024};
RA   Wagner M.;
RT   "Active sludge and wastewater microbial communities from Klosterneuburg,
RT   Austria.";
RL   Submitted (MAY-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:PXW88894.1}.
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DR   EMBL; QJJP01000006; PXW88894.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V3W6T5; -.
DR   UniPathway; UPA00077; UER00155.
DR   Proteomes; UP000248024; 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.
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:PXW88894.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..137
FT                   /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT                   /evidence="ECO:0000259|Pfam:PF01288"
SQ   SEQUENCE   165 AA;  18323 MW;  70452D4576D3D1EF CRC64;
     MNKQPSQAFI ALGSNLENPI SQIQQAFEEL KQLPGTCLMK QSSLYQSAPV GRLDQPDFIN
     AVALIKTCLA PHDLLNALLA IEQNHGRVRE SLNAPRTLDL DILLYDDLQC HDEKLTLPHP
     RMLQRAFVLK PLMEIAPDCH IPGHGHIAPL LATCNGQQLK QIKAI
//
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