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Database: UniProt
Entry: E6S9V8_INTC7
LinkDB: E6S9V8_INTC7
Original site: E6S9V8_INTC7 
ID   E6S9V8_INTC7            Unreviewed;       295 AA.
AC   E6S9V8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
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   OrderedLocusNames=Intca_0603 {ECO:0000313|EMBL:ADU47148.1};
OS   Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / NBRC
OS   12989 / 7 KIP).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU47148.1, ECO:0000313|Proteomes:UP000008914};
RN   [1] {ECO:0000313|EMBL:ADU47148.1, ECO:0000313|Proteomes:UP000008914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC   {ECO:0000313|Proteomes:UP000008914};
RX   PubMed=21304734; DOI=10.4056/sigs.1263355;
RA   Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S., Cheng J.F.,
RA   Detter C., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Pukall R., Sikorski J.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Intrasporangium calvum type strain (7 KIP).";
RL   Stand. Genomic Sci. 3:294-303(2010).
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=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; CP002343; ADU47148.1; -; Genomic_DNA.
DR   RefSeq; WP_013491469.1; NC_014830.1.
DR   AlphaFoldDB; E6S9V8; -.
DR   STRING; 710696.Intca_0603; -.
DR   KEGG; ica:Intca_0603; -.
DR   eggNOG; COG0801; Bacteria.
DR   eggNOG; COG1539; Bacteria.
DR   HOGENOM; CLU_023499_1_0_11; -.
DR   OrthoDB; 9808041at2; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000008914; 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: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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909,
KW   ECO:0000256|RuleBase:RU362079}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Lyase {ECO:0000256|RuleBase:RU362079};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008914};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..117
FT                   /note="Dihydroneopterin aldolase/epimerase"
FT                   /evidence="ECO:0000259|SMART:SM00905"
SQ   SEQUENCE   295 AA;  31568 MW;  D26AFB77665FD355 CRC64;
     MTDEIVLRGV TARGHHGVLD AEKRDGQTFV VDVHLSLDLS RAGQTDDLSA TVNYAEVASL
     IVARITGPSF DLVERLAEVI ADDVLDFGLV DSVEVVVHKP EAPVGHPFTD VEVRVRRSRG
     PRAVIALGSN LGDRGRTLSL AVDALRSLPG FTVTSVSPIV ESEPVGGPDQ PPYLNAVVVG
     RTTLVAADLL DALHRIEAAH GRTRDVRWDA RTLDLDLIQV GTPGSAEEVV SDDETLTLPH
     PRAGERAFVL VPWAAADPDA RLRLGSADQE IRPVRQILGG LDQSGVRPGP EWGQS
//
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