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Database: UniProt
Entry: A0A2S9QSR3_9MICO
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ID   A0A2S9QSR3_9MICO        Unreviewed;       173 AA.
AC   A0A2S9QSR3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=B4915_00655 {ECO:0000313|EMBL:PRI12609.1};
OS   Leucobacter massiliensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=1686285 {ECO:0000313|EMBL:PRI12609.1, ECO:0000313|Proteomes:UP000238650};
RN   [1] {ECO:0000313|EMBL:PRI12609.1, ECO:0000313|Proteomes:UP000238650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=122RC15 {ECO:0000313|EMBL:PRI12609.1,
RC   ECO:0000313|Proteomes:UP000238650};
RX   PubMed=29204283;
RA   Leangapichart T., Gautret P., Nguyen T.T., Armstrong N., Rolain J.M.;
RT   "Genome sequence of 'Leucobacter massiliensis' sp. nov. isolated from human
RT   pharynx after travel to the 2014 Hajj.";
RL   New Microbes New Infect 21:42-48(2017).
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:PRI12609.1}.
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DR   EMBL; MWZD01000008; PRI12609.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S9QSR3; -.
DR   OrthoDB; 9808041at2; -.
DR   UniPathway; UPA00077; UER00155.
DR   Proteomes; UP000238650; 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.
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:PRI12609.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238650};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..141
FT                   /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT                   /evidence="ECO:0000259|Pfam:PF01288"
SQ   SEQUENCE   173 AA;  18780 MW;  64CB76852B7B20E0 CRC64;
     MIAQIVPVLF AFGANLGDRG ETIRAAQRAL AAAPGIRDFS ASPLRETIAL TERGPDPEAP
     RYLNGVASAQ TALTPHELLD LTQRLEADHG RVRDARWGDR TLDIDLILYG GRVVRDERLT
     IPHPRAHERD FVLAPWLALD PDAVLMGHGR VDALLARIGD TTAPFAEPGD AQA
//
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