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Database: UniProt
Entry: A0A1G5J933_9RHOB
LinkDB: A0A1G5J933_9RHOB
Original site: A0A1G5J933_9RHOB 
ID   A0A1G5J933_9RHOB        Unreviewed;       147 AA.
AC   A0A1G5J933;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=SAMN05660710_03072 {ECO:0000313|EMBL:SCY84865.1};
OS   Paracoccus tibetensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=336292 {ECO:0000313|EMBL:SCY84865.1, ECO:0000313|Proteomes:UP000199502};
RN   [1] {ECO:0000313|EMBL:SCY84865.1, ECO:0000313|Proteomes:UP000199502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.8925 {ECO:0000313|EMBL:SCY84865.1,
RC   ECO:0000313|Proteomes:UP000199502};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FMVT01000011; SCY84865.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5J933; -.
DR   STRING; 336292.SAMN05660710_03072; -.
DR   UniPathway; UPA00077; UER00155.
DR   Proteomes; UP000199502; 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   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:SCY84865.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199502};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..109
FT                   /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT                   /evidence="ECO:0000259|Pfam:PF01288"
SQ   SEQUENCE   147 AA;  15696 MW;  3E98D42F9D5EE67C CRC64;
     MPAGSGPDFA NAVALIRTSL GPEALLSCLH EIEAEAGRDR SGGRWSARVL DLDLIALDDR
     VLPDAATLRG WIDLPPAEQA RRAPAHLLLP HPRMQDRAFV LAPLCEIAPF WRHPLTGASA
     AQMLVDLGPD ALAGMRPLPW PPAVPAA
//
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