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Database: UniProt
Entry: A0A0B0H1J3_SOVGS
LinkDB: A0A0B0H1J3_SOVGS
Original site: A0A0B0H1J3_SOVGS 
ID   A0A0B0H1J3_SOVGS        Unreviewed;       157 AA.
AC   A0A0B0H1J3;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
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   ORFNames=BOV88_00725 {ECO:0000313|EMBL:OOY36156.1}, JV46_25750
GN   {ECO:0000313|EMBL:KHF24088.1};
OS   Solemya velum gill symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=2340 {ECO:0000313|EMBL:KHF24088.1, ECO:0000313|Proteomes:UP000030856};
RN   [1] {ECO:0000313|EMBL:KHF24088.1, ECO:0000313|Proteomes:UP000030856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH {ECO:0000313|EMBL:KHF24088.1,
RC   ECO:0000313|Proteomes:UP000030856};
RX   PubMed=25342549; DOI=10.1186/1471-2164-15-924;
RA   Dmytrenko O., Russell S.L., Loo W.T., Fontanez K.M., Liao L., Roeselers G.,
RA   Sharma R., Stewart F.J., Newton I.L., Woyke T., Wu D., Lang J.M.,
RA   Eisen J.A., Cavanaugh C.M.;
RT   "The genome of the intracellular bacterium of the coastal bivalve, Solemya
RT   velum: a blueprint for thriving in and out of symbiosis.";
RL   BMC Genomics 15:924-924(2014).
RN   [2] {ECO:0000313|EMBL:OOY36156.1, ECO:0000313|Proteomes:UP000190962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MA-KB16 {ECO:0000313|EMBL:OOY36156.1};
RA   Russell S.L., Corbett-Detig R.B., Cavanaugh C.M.;
RT   "Mixed transmission modes and dynamic genome evolution in an obligate
RT   animal-bacterial symbiosis.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:KHF24088.1}.
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DR   EMBL; JRAA01000003; KHF24088.1; -; Genomic_DNA.
DR   EMBL; MPNX01000001; OOY36156.1; -; Genomic_DNA.
DR   RefSeq; WP_043118124.1; NZ_MPRZ01000001.1.
DR   AlphaFoldDB; A0A0B0H1J3; -.
DR   STRING; 2340.JV46_25750; -.
DR   GeneID; 67402342; -.
DR   PATRIC; fig|2340.3.peg.2165; -.
DR   eggNOG; COG0801; Bacteria.
DR   OrthoDB; 9790168at2; -.
DR   UniPathway; UPA00077; UER00155.
DR   Proteomes; UP000030856; Unassembled WGS sequence.
DR   Proteomes; UP000190962; 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:SF2; 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   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:KHF24088.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030856};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KHF24088.1}.
FT   DOMAIN          6..129
FT                   /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT                   /evidence="ECO:0000259|Pfam:PF01288"
SQ   SEQUENCE   157 AA;  17874 MW;  ADA13FED7E810D48 CRC64;
     MSRIWLSIGS NIERELHITE ALSQLESELG KAILSPYYES PAEGFEGPDF INLVAGYDTD
     KRPAELIKLF NSIESGLGRT RTEKKFSSRT IDIDLLTYGD QVIEVMGKQL PRDDILKYSF
     VLKPLADVAA DEVHVLTGKT YQQHWDEFTP KDRLIRL
//
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