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Bifunctional folate synthesis protein [Includes: Dihydroneopterin aldolase (DHNA) (EC 4.1.2.25) (7,8-dihydroneopterin aldolase); 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (EC 2.7.6.3) (6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase) (PPPK) (7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase) (HPPK)]

 SULD_STRPN              Reviewed;         270 AA.
P22291; O33697;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
26-SEP-2001, sequence version 3.
05-JUL-2017, entry version 123.
RecName: Full=Bifunctional folate synthesis protein;
Includes:
RecName: Full=Dihydroneopterin aldolase {ECO:0000303|PubMed:8385663};
Short=DHNA {ECO:0000303|PubMed:8385663};
EC=4.1.2.25 {ECO:0000269|PubMed:8385663};
AltName: Full=7,8-dihydroneopterin aldolase;
Includes:
RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase;
EC=2.7.6.3 {ECO:0000269|PubMed:2168367, ECO:0000269|PubMed:8385663};
AltName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000303|PubMed:2168367};
Short=PPPK {ECO:0000303|PubMed:2168367};
AltName: Full=7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase;
Short=HPPK {ECO:0000303|PubMed:8385663};
Name=sulD {ECO:0000303|PubMed:2168367}; OrderedLocusNames=SP_0292;
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=170187;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-13, CATALYTIC
ACTIVITY, AND SUBUNIT.
STRAIN=708;
PubMed=2168367; DOI=10.1128/jb.172.9.4766-4774.1990;
Lopez P., Greenberg B., Lacks S.A.;
"DNA sequence of folate biosynthesis gene sulD, encoding
hydroxymethyldihydropterin pyrophosphokinase in Streptococcus
pneumoniae, and characterization of the enzyme.";
J. Bacteriol. 172:4766-4774(1990).
[2]
SEQUENCE REVISION TO 156-170.
STRAIN=772;
PubMed=7798151; DOI=10.1128/jb.177.1.66-74.1995;
Lacks S.A., Greenberg B., Lopez P.;
"A cluster of four genes encoding enzymes for five steps in the folate
biosynthetic pathway of Streptococcus pneumoniae.";
J. Bacteriol. 177:66-74(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-334 / TIGR4;
PubMed=11463916; DOI=10.1126/science.1061217;
Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T.,
Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C.,
Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.;
"Complete genome sequence of a virulent isolate of Streptococcus
pneumoniae.";
Science 293:498-506(2001).
[4]
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND CHARACTERIZATION.
PubMed=8385663; DOI=10.1128/jb.175.8.2214-2220.1993;
Lopez P., Lacks S.A.;
"A bifunctional protein in the folate biosynthetic pathway of
Streptococcus pneumoniae with dihydroneopterin aldolase and
hydroxymethyldihydropterin pyrophosphokinase activities.";
J. Bacteriol. 175:2214-2220(1993).
-!- FUNCTION: Catalyzes two sequential steps of tetrahydrofolate
biosynthesis, the conversion of 7,8-dihydroneopterin to 6-
hydroxymethyl-7,8-dihydropterin diphosphate.
{ECO:0000269|PubMed:8385663}.
-!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-
dihydropterin + glycolaldehyde. {ECO:0000269|PubMed:8385663}.
-!- CATALYTIC ACTIVITY: ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP
+ 6-hydroxymethyl-7,8-dihydropterin diphosphate.
{ECO:0000269|PubMed:2168367, ECO:0000269|PubMed:8385663}.
-!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-
amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate
from 7,8-dihydroneopterin triphosphate: step 3/4.
-!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-
amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate
from 7,8-dihydroneopterin triphosphate: step 4/4.
-!- SUBUNIT: Homotrimer or homotetramer. {ECO:0000269|PubMed:2168367,
ECO:0000269|PubMed:8385663}.
-!- INTERACTION:
Q97NV3:groS; NbExp=2; IntAct=EBI-2207011, EBI-2206949;
-!- SIMILARITY: In the N-terminal section; belongs to the DHNA family.
{ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the HPPK family.
{ECO:0000305}.
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EMBL; U16156; AAB63947.1; -; Genomic_DNA.
EMBL; AE005672; AAK74470.1; -; Genomic_DNA.
PIR; A36704; A36704.
PIR; E95034; E95034.
PIR; E97905; E97905.
RefSeq; WP_000372529.1; NZ_AKVY01000001.1.
ProteinModelPortal; P22291; -.
SMR; P22291; -.
IntAct; P22291; 1.
EnsemblBacteria; AAK74470; AAK74470; SP_0292.
KEGG; spn:SP_0292; -.
eggNOG; ENOG4105K8U; Bacteria.
eggNOG; COG0801; LUCA.
eggNOG; COG1539; LUCA.
HOGENOM; HOG000019668; -.
KO; K13940; -.
OMA; IKKPWAP; -.
UniPathway; UPA00077; UER00154.
UniPathway; UPA00077; UER00155.
Proteomes; UP000000585; Chromosome.
GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-EC.
GO; GO:0102083; F:7,8-dihydromonapterin aldolase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-EC.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd00534; DHNA_DHNTPE; 1.
CDD; cd00483; HPPK; 1.
Gene3D; 3.30.70.560; -; 1.
InterPro; IPR006156; Dihydroneopterin_aldolase.
InterPro; IPR006157; FolB_dom.
InterPro; IPR000550; Hppk.
Pfam; PF02152; FolB; 1.
Pfam; PF01288; HPPK; 1.
SMART; SM00905; FolB; 1.
SUPFAM; SSF55083; SSF55083; 1.
TIGRFAMs; TIGR00525; folB; 1.
TIGRFAMs; TIGR00526; folB_dom; 1.
TIGRFAMs; TIGR01498; folK; 1.
PROSITE; PS00794; HPPK; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Direct protein sequencing;
Folate biosynthesis; Kinase; Lyase; Magnesium; Metal-binding;
Multifunctional enzyme; Nucleotide-binding; Transferase.
CHAIN 1 270 Bifunctional folate synthesis protein.
/FTId=PRO_0000168244.
NP_BIND 160 163 ATP. {ECO:0000250|UniProtKB:P26281}.
NP_BIND 171 173 ATP. {ECO:0000250|UniProtKB:P26281}.
NP_BIND 192 195 ATP. {ECO:0000250|UniProtKB:P26281}.
NP_BIND 200 215 ATP. {ECO:0000250|UniProtKB:P26281}.
NP_BIND 227 233 ATP. {ECO:0000250|UniProtKB:P26281}.
NP_BIND 238 240 ATP. {ECO:0000250|UniProtKB:P26281}.
REGION 1 119 DHNA.
REGION 72 73 Substrate binding.
{ECO:0000250|UniProtKB:P0AC16}.
REGION 120 270 HPPK.
ACT_SITE 99 99 Proton donor/acceptor; for DHNA activity.
{ECO:0000250|UniProtKB:P0AC16}.
METAL 212 212 Magnesium 1.
{ECO:0000250|UniProtKB:P26281}.
METAL 212 212 Magnesium 2.
{ECO:0000250|UniProtKB:P26281}.
METAL 214 214 Magnesium 1.
{ECO:0000250|UniProtKB:P26281}.
METAL 214 214 Magnesium 2.
{ECO:0000250|UniProtKB:P26281}.
BINDING 21 21 Substrate.
{ECO:0000250|UniProtKB:P0AC16}.
BINDING 53 53 Substrate.
{ECO:0000250|UniProtKB:P0AC16}.
CONFLICT 29 29 V -> I (in Ref. 1; AAB63947).
{ECO:0000305}.
CONFLICT 86 86 F -> S (in Ref. 1; AAB63947).
{ECO:0000305}.
SEQUENCE 270 AA; 31143 MW; 1AAD0229E639A827 CRC64;
MDQLQIKDLE MFAYHGLFPS EKELGQKFVV SAILSYDMTK AATDLDLTAS VHYGELCQQW
TTWFQETSED LIETVAYKLV ERTFEFYPLV QEMKLELKKP WAPVHLSLDT CSVTIHRRKQ
RAFIALGSNM GDKQANLKQA IDKLRARGIH ILKESSVLAT EPWGGVEQDS FANQVVEVET
WLPAQDLLET LLAIESELGR VREVHWGPRL IDLDLLFVED QILYTDDLIL PHPYIAERLF
VLESLQEIAP HFIHPILKQP IRNLYDALKK


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