ID K4R6V0_STRDJ Unreviewed; 203 AA.
AC K4R6V0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase {ECO:0000256|ARBA:ARBA00013253};
DE EC=2.7.6.3 {ECO:0000256|ARBA:ARBA00013253};
GN Name=folK {ECO:0000313|EMBL:CCK28434.1};
GN ORFNames=BN159_4055 {ECO:0000313|EMBL:CCK28434.1};
OS Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK28434.1, ECO:0000313|Proteomes:UP000008043};
RN [1] {ECO:0000313|EMBL:CCK28434.1, ECO:0000313|Proteomes:UP000008043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC {ECO:0000313|Proteomes:UP000008043};
RX PubMed=23043000; DOI=10.1128/JB.01592-12;
RA Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA Pelzer S., Kalinowski J., Mack M.;
RT "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT heterologous production of the unique antibiotic roseoflavin.";
RL J. Bacteriol. 194:6818-6827(2012).
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}.
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DR EMBL; HE971709; CCK28434.1; -; Genomic_DNA.
DR RefSeq; WP_015658786.1; NC_020504.1.
DR AlphaFoldDB; K4R6V0; -.
DR STRING; 1214101.BN159_4055; -.
DR KEGG; sdv:BN159_4055; -.
DR PATRIC; fig|1214101.3.peg.4106; -.
DR eggNOG; COG0801; Bacteria.
DR HOGENOM; CLU_097916_0_0_11; -.
DR OrthoDB; 9808041at2; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000008043; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCK28434.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008043};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 124..135
FT /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT /evidence="ECO:0000259|PROSITE:PS00794"
SQ SEQUENCE 203 AA; 21999 MW; 7AE39A601F75CA1E CRC64;
MTAFFAGGHS DPTVQPVPAS VVEQVDAADT TLHNPRRAVI SLGSNLGNRL ENLQGAIDAM
EDTPGVRIKA VSPVYETEPW GVEPGSQPSY FNAVVVLKTT LPPSSLLERA QAVEEAFHRV
RDERWGPRTL DVDIVAYADV VTDDPVLTLP HPRAHERAFV LAPWYDVEPG AQLPGRGAVA
DLLGTLTREG VTPRADLELR LPE
//
