ID Q3SH85_THIDA Unreviewed; 168 AA.
AC Q3SH85;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, 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 OrderedLocusNames=Tbd_2051 {ECO:0000313|EMBL:AAZ98004.1};
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415 {ECO:0000313|EMBL:AAZ98004.1, ECO:0000313|Proteomes:UP000008291};
RN [1] {ECO:0000313|EMBL:AAZ98004.1, ECO:0000313|Proteomes:UP000008291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259 {ECO:0000313|EMBL:AAZ98004.1,
RC ECO:0000313|Proteomes:UP000008291};
RX PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ98004.1; -; Genomic_DNA.
DR RefSeq; WP_011312563.1; NC_007404.1.
DR AlphaFoldDB; Q3SH85; -.
DR STRING; 292415.Tbd_2051; -.
DR KEGG; tbd:Tbd_2051; -.
DR eggNOG; COG0801; Bacteria.
DR HOGENOM; CLU_097916_2_3_4; -.
DR OrthoDB; 9808041at2; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000008291; Chromosome.
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:AAZ98004.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008291};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAZ98004.1}.
FT DOMAIN 89..100
FT /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT /evidence="ECO:0000259|PROSITE:PS00794"
SQ SEQUENCE 168 AA; 17997 MW; 7417E60E63A386C5 CRC64;
MKVVATIGLG ANLNDPAAQV EYALAELDRL PATRLLARSS LYASSPVGYV DQPDFINAVA
QVETGLAPRA LLAALLDIEQ RHGRERSFRN APRTLDLDLL LYGSARFHED GLTLPHPRMH
ERAFVLLPLL EIAAQTVIPG RGPAEDWLAA ASGQNVALLP PSPAAAHA
//
