ID A0A428MV97_9BACI Unreviewed; 177 AA.
AC A0A428MV97;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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:RSL30060.1};
GN ORFNames=D7Z54_28145 {ECO:0000313|EMBL:RSL30060.1};
OS Salibacterium salarium.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=284579 {ECO:0000313|EMBL:RSL30060.1, ECO:0000313|Proteomes:UP000275076};
RN [1] {ECO:0000313|EMBL:RSL30060.1, ECO:0000313|Proteomes:UP000275076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IM0101 {ECO:0000313|EMBL:RSL30060.1,
RC ECO:0000313|Proteomes:UP000275076};
RA Yamprayoonswat W., Boonvisut S., Jumpathong W., Sittihan S., Ruangsuj P.,
RA Wanthongcharoen S., Thongpramul N., Pimmason S., Yu B., Yasawong M.;
RT "Draft genome sequence of Bacillus salarius IM0101, isolated from a
RT hypersaline soil in Inner Mongolia, China.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RSL30060.1}.
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DR EMBL; RBVX01000044; RSL30060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428MV97; -.
DR OrthoDB; 9808041at2; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000275076; 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.
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:RSL30060.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000275076};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RSL30060.1}.
FT DOMAIN 89..100
FT /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT /evidence="ECO:0000259|PROSITE:PS00794"
SQ SEQUENCE 177 AA; 20397 MW; 81987DEF0A8D6AF8 CRC64;
MTNHLFLALG SNVGDRESYL RQAVEKLNQH PDVCVTQLSS IYETAPVGVT DQPSFFNMVL
RLKTTLNASE VLRTTQKMEQ DLDRKREKRW GPRTIDLDIL LFNDENIKME DLYIPHPRMH
ERAFVLVPLN EIAGDNYVSS YNQYISEMTS QLSDREKEGV HLWKSCTGPE GFGLFES
//
