ID A0A0A8JFI1_BACSX Unreviewed; 165 AA.
AC A0A0A8JFI1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ORFNames=OXB_1051 {ECO:0000313|EMBL:BAQ09523.1};
OS Bacillus sp. (strain OxB-1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=98228 {ECO:0000313|EMBL:BAQ09523.1, ECO:0000313|Proteomes:UP000031651};
RN [1] {ECO:0000313|Proteomes:UP000031651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OxB-1 {ECO:0000313|Proteomes:UP000031651};
RA Yamaguchi T., Asano Y.;
RT "Complete genome of an aldoxime degrader Bacillus sp. OxB-1.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAQ09523.1, ECO:0000313|Proteomes:UP000031651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OxB-1 {ECO:0000313|EMBL:BAQ09523.1,
RC ECO:0000313|Proteomes:UP000031651};
RA Yamaguchi T., Asano Y.;
RT "Complete Genome Sequence of an Aldoxime Degrader, Bacillus sp. OxB-1.";
RL Genome Announc. 3:e00025-15(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-
CC 6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841,
CC ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000198};
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; AP013294; BAQ09523.1; -; Genomic_DNA.
DR RefSeq; WP_041072522.1; NZ_AP013294.1.
DR AlphaFoldDB; A0A0A8JFI1; -.
DR STRING; 98228.OXB_1051; -.
DR KEGG; baco:OXB_1051; -.
DR HOGENOM; CLU_097916_1_2_9; -.
DR OrthoDB; 9808041at2; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000031651; 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:BAQ09523.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031651};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 88..99
FT /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT /evidence="ECO:0000259|PROSITE:PS00794"
SQ SEQUENCE 165 AA; 18710 MW; C33B65E5FD4C835B CRC64;
MNVAYLSIGS NIGDRLRHLQ ESVKALHSQE GIEVTAVSSI YETEPIGYIG QADFLNMAVE
LQTDLDPYAL LNVCQQIEYD QGRKRLIRWG PRTIDLDILL YNNENIESEN LIIPHPRMQE
RAFVLVPLFE IAPELAISGK AVQTNGVRLW KKIDEVTSFL SETLL
//
