ID E9FIJ7_9STRE Unreviewed; 273 AA.
AC E9FIJ7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Bifunctional folate synthesis protein {ECO:0000256|RuleBase:RU362079};
DE Includes:
DE RecName: Full=Dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE Short=DHNA {ECO:0000256|RuleBase:RU362079};
DE EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
DE AltName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE Includes:
DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase {ECO:0000256|RuleBase:RU362079};
DE EC=2.7.6.3 {ECO:0000256|RuleBase:RU362079};
DE AltName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000256|RuleBase:RU362079};
DE Short=PPPK {ECO:0000256|RuleBase:RU362079};
DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase {ECO:0000256|RuleBase:RU362079};
DE Short=HPPK {ECO:0000256|RuleBase:RU362079};
GN Name=folK {ECO:0000313|EMBL:EFX56118.1};
GN ORFNames=HMPREF0849_01522 {ECO:0000313|EMBL:EFX56118.1};
OS Streptococcus sp. C300.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=563036 {ECO:0000313|EMBL:EFX56118.1, ECO:0000313|Proteomes:UP000003809};
RN [1] {ECO:0000313|EMBL:EFX56118.1, ECO:0000313|Proteomes:UP000003809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C300 {ECO:0000313|EMBL:EFX56118.1,
RC ECO:0000313|Proteomes:UP000003809};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S., Surette M.G.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. C300.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin +
CC glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001,
CC ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25;
CC Evidence={ECO:0000256|RuleBase:RU362079};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 3/4.
CC {ECO:0000256|RuleBase:RU362079}.
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 DHNA family.
CC {ECO:0000256|RuleBase:RU362079}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DHNA family.
CC {ECO:0000256|ARBA:ARBA00009640}.
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DR EMBL; GL732469; EFX56118.1; -; Genomic_DNA.
DR RefSeq; WP_000372503.1; NZ_GL732469.1.
DR AlphaFoldDB; E9FIJ7; -.
DR HOGENOM; CLU_023499_0_0_9; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000003809; 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:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00534; DHNA_DHNTPE; 1.
DR CDD; cd00483; HPPK; 1.
DR Gene3D; 3.30.1130.10; -; 1.
DR Gene3D; 3.30.70.560; 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK; 1.
DR InterPro; IPR006156; Dihydroneopterin_aldolase.
DR InterPro; IPR006157; FolB_dom.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR NCBIfam; TIGR00525; folB; 1.
DR NCBIfam; TIGR00526; folB_dom; 1.
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; PF02152; FolB; 1.
DR Pfam; PF01288; HPPK; 1.
DR SMART; SM00905; FolB; 1.
DR SUPFAM; SSF55083; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK; 1.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
DR PROSITE; PS00794; HPPK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909,
KW ECO:0000256|RuleBase:RU362079};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFX56118.1};
KW Lyase {ECO:0000256|RuleBase:RU362079};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFX56118.1}.
FT DOMAIN 205..216
FT /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT /evidence="ECO:0000259|PROSITE:PS00794"
SQ SEQUENCE 273 AA; 31431 MW; 4DE624B09A6570C4 CRC64;
MDQLQIKDLE IFAYHGLFPS EKELGQKFVI SASLSYDMTK AATELDLTAS VHYGELCQQW
TTWFQESTED LIETVAYKLV ERTFETYPLV QEIELELKKP WAPVHLPLDT CSVTIHRRKQ
RAFIALGSNM GDKEANLEQA IDKLRARGIH ILKESSVLAT EPWGGVDQDS FANQVIEVET
WLPAPVLLET LLAIESEMGR VREVHWGPRL IDLDLLFMED QIIYTDELIL PHPYIAERLF
VLEPLVEIAP HFIHPILKQP IRYLVDQLEQ ENA
//
