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Dihydropteroate synthase (DHPS) (EC 2.5.1.15) (Dihydropteroate pyrophosphorylase)

 DHPS1_MYCTU             Reviewed;         280 AA.
P9WND1; L0TG01; O06274; P0A578;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
28-MAR-2018, entry version 26.
RecName: Full=Dihydropteroate synthase {ECO:0000303|PubMed:10542185};
Short=DHPS {ECO:0000303|PubMed:10542185};
EC=2.5.1.15 {ECO:0000269|PubMed:10542185, ECO:0000269|PubMed:23118010, ECO:0000269|PubMed:23779105};
AltName: Full=Dihydropteroate pyrophosphorylase;
Name=folP1; OrderedLocusNames=Rv3608c; ORFNames=MTCY07H7B.14;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND SUBUNIT.
STRAIN=H37Rv;
PubMed=10542185;
Nopponpunth V., Sirawaraporn W., Greene P.J., Santi D.V.;
"Cloning and expression of Mycobacterium tuberculosis and
Mycobacterium leprae dihydropteroate synthase in Escherichia coli.";
J. Bacteriol. 181:6814-6821(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[4]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
ENZYME REGULATION.
STRAIN=H37Rv;
PubMed=23779105; DOI=10.1074/jbc.M113.475798;
Zheng J., Rubin E.J., Bifani P., Mathys V., Lim V., Au M., Jang J.,
Nam J., Dick T., Walker J.R., Pethe K., Camacho L.R.;
"para-Aminosalicylic acid is a prodrug targeting dihydrofolate
reductase in Mycobacterium tuberculosis.";
J. Biol. Chem. 288:23447-23456(2013).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=H37Rv;
PubMed=23118010; DOI=10.1126/science.1228980;
Chakraborty S., Gruber T., Barry C.E. III, Boshoff H.I., Rhee K.Y.;
"Para-aminosalicylic acid acts as an alternative substrate of folate
metabolism in Mycobacterium tuberculosis.";
Science 339:88-91(2013).
[6]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS
AND PTERIN MONOPHOSPHATE, AND COFACTOR.
PubMed=11007651; DOI=10.1006/jmbi.2000.4094;
Baca A.M., Sirawaraporn R., Turley S., Sirawaraporn W., Hol W.G.J.;
"Crystal structure of Mycobacterium tuberculosis 7,8-dihydropteroate
synthase in complex with pterin monophosphate: new insight into the
enzymatic mechanism and sulfa-drug action.";
J. Mol. Biol. 302:1193-1212(2000).
[7]
ERRATUM.
Baca A.M., Sirawaraporn R., Turley S., Sirawaraporn W., Hol W.G.J.;
J. Mol. Biol. 303:843-843(2000).
-!- FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA)
with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to
form 7,8-dihydropteroate (H2Pte), the immediate precursor of
folate derivatives. {ECO:0000269|PubMed:10542185,
ECO:0000269|PubMed:23118010, ECO:0000269|PubMed:23779105}.
-!- FUNCTION: Is involved in the bioactivation of the antituberculous
drug para-aminosalicylic acid (PAS). PAS is a close structural
analog of pABA and acts as an alternative substrate for DHPS,
leading to hydroxy-dihydropteroate (H2PtePAS). Metabolomic studies
show that PAS, despite its in vitro activity as a competitive
inhibitor of DHPS, does not inhibit growth of M.tuberculosis by
inhibiting DHPS. PAS exerts its antimycobacterial activity through
its effects on M.tuberculosis folate metabolism downstream of
DHPS. PAS poisons folate-dependent pathways not only by serving as
a replacement substrate for DHPS but also by the products of that
reaction serving as replacement substrates and/or inhibitors of
subsequent enzymes. {ECO:0000269|PubMed:23118010,
ECO:0000269|PubMed:23779105}.
-!- CATALYTIC ACTIVITY: 6-hydroxymethyl-7,8-dihydropterin diphosphate
+ 4-aminobenzoate = diphosphate + dihydropteroate.
{ECO:0000269|PubMed:10542185, ECO:0000269|PubMed:23118010,
ECO:0000269|PubMed:23779105}.
-!- CATALYTIC ACTIVITY: 6-hydroxymethyl-7,8-dihydropterin diphosphate
+ 4-aminosalicylate = diphosphate + hydroxy-dihydropteroate.
{ECO:0000269|PubMed:23118010}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000305|PubMed:11007651};
Note=Magnesium is required for activity, even if it seems to
interact primarily with the substrate. {ECO:0000305};
-!- ENZYME REGULATION: Is potently inhibited by the sulfone dapsone
and the two sulfonamides sulfamethoxazole and
sulfamethoxypyridazine, with Kis in the range of 12 to 32 nM. Is
only poorly inhibited by p-aminosalicylate (PAS)
(PubMed:10542185). The inhibition of DHPS by sulfathiazole
antagonizes PAS-mediated growth inhibition and therefore confers
resistance to PAS (PubMed:23779105). {ECO:0000269|PubMed:10542185,
ECO:0000269|PubMed:23779105}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.37 uM for 4-aminobenzoate {ECO:0000269|PubMed:10542185};
KM=1.03 uM for 6-hydroxymethyl-7,8-dihydropterin diphosphate
{ECO:0000269|PubMed:10542185};
KM=0.6 uM for 4-aminobenzoate {ECO:0000269|PubMed:23118010};
KM=1.8 uM for para-aminosalicylate
{ECO:0000269|PubMed:23118010};
KM=11.4 uM for 4-aminobenzoate {ECO:0000269|PubMed:23779105};
KM=17.7 uM for para-aminosalicylate
{ECO:0000269|PubMed:23779105};
Note=kcat is 35 min(-1) (PubMed:10542185). kcat is 28 min(-1)
with pABA as substrate, and 45 min(-1) with PAS as substrate
(PubMed:23118010). {ECO:0000269|PubMed:10542185,
ECO:0000269|PubMed:23118010};
pH dependence:
Optimum pH is 8. {ECO:0000269|PubMed:10542185};
-!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
{ECO:0000305|PubMed:10542185}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10542185}.
-!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF117617; AAF06724.1; -; Genomic_DNA.
EMBL; AL123456; CCP46431.1; -; Genomic_DNA.
PIR; A70956; A70956.
RefSeq; WP_003899596.1; NZ_KK339374.1.
RefSeq; YP_177997.1; NC_000962.3.
PDB; 1EYE; X-ray; 1.70 A; A=1-280.
PDBsum; 1EYE; -.
ProteinModelPortal; P9WND1; -.
SMR; P9WND1; -.
STRING; 83332.Rv3608c; -.
PaxDb; P9WND1; -.
EnsemblBacteria; CCP46431; CCP46431; Rv3608c.
GeneID; 885831; -.
KEGG; mtu:Rv3608c; -.
TubercuList; Rv3608c; -.
eggNOG; ENOG4105EEI; Bacteria.
eggNOG; COG0294; LUCA.
KO; K00796; -.
OMA; WAVRVHD; -.
PhylomeDB; P9WND1; -.
SABIO-RK; P9WND1; -.
UniPathway; UPA00077; UER00156.
Proteomes; UP000001584; Chromosome.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0004156; F:dihydropteroate synthase activity; IDA:MTBBASE.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0040007; P:growth; IMP:MTBBASE.
GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IDA:MTBBASE.
CDD; cd00739; DHPS; 1.
Gene3D; 3.20.20.20; -; 1.
InterPro; IPR006390; DHP_synth.
InterPro; IPR011005; Dihydropteroate_synth-like.
InterPro; IPR000489; Pterin-binding_dom.
Pfam; PF00809; Pterin_bind; 1.
SUPFAM; SSF51717; SSF51717; 1.
TIGRFAMs; TIGR01496; DHPS; 1.
PROSITE; PS00792; DHPS_1; 1.
PROSITE; PS00793; DHPS_2; 1.
PROSITE; PS50972; PTERIN_BINDING; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Folate biosynthesis; Magnesium;
Metal-binding; Reference proteome; Transferase.
CHAIN 1 280 Dihydropteroate synthase.
/FTId=PRO_0000168215.
DOMAIN 1 265 Pterin-binding. {ECO:0000255|PROSITE-
ProRule:PRU00334}.
REGION 253 255 6-hydroxymethyl-7,8-dihydropterin
diphosphate binding.
{ECO:0000244|PDB:1EYE,
ECO:0000305|PubMed:11007651}.
METAL 13 13 Magnesium. {ECO:0000269|PubMed:11007651}.
BINDING 21 21 6-hydroxymethyl-7,8-dihydropterin
diphosphate. {ECO:0000244|PDB:1EYE,
ECO:0000305|PubMed:11007651}.
BINDING 86 86 6-hydroxymethyl-7,8-dihydropterin
diphosphate. {ECO:0000244|PDB:1EYE,
ECO:0000305|PubMed:11007651}.
BINDING 105 105 6-hydroxymethyl-7,8-dihydropterin
diphosphate. {ECO:0000244|PDB:1EYE,
ECO:0000305|PubMed:11007651}.
BINDING 177 177 6-hydroxymethyl-7,8-dihydropterin
diphosphate. {ECO:0000244|PDB:1EYE,
ECO:0000305|PubMed:11007651}.
BINDING 213 213 6-hydroxymethyl-7,8-dihydropterin
diphosphate. {ECO:0000244|PDB:1EYE,
ECO:0000305|PubMed:11007651}.
STRAND 7 13 {ECO:0000244|PDB:1EYE}.
HELIX 28 40 {ECO:0000244|PDB:1EYE}.
STRAND 44 49 {ECO:0000244|PDB:1EYE}.
HELIX 66 78 {ECO:0000244|PDB:1EYE}.
STRAND 83 86 {ECO:0000244|PDB:1EYE}.
HELIX 90 98 {ECO:0000244|PDB:1EYE}.
STRAND 103 106 {ECO:0000244|PDB:1EYE}.
TURN 107 110 {ECO:0000244|PDB:1EYE}.
HELIX 116 123 {ECO:0000244|PDB:1EYE}.
STRAND 127 130 {ECO:0000244|PDB:1EYE}.
HELIX 149 166 {ECO:0000244|PDB:1EYE}.
HELIX 171 173 {ECO:0000244|PDB:1EYE}.
STRAND 174 177 {ECO:0000244|PDB:1EYE}.
HELIX 186 194 {ECO:0000244|PDB:1EYE}.
HELIX 196 200 {ECO:0000244|PDB:1EYE}.
STRAND 206 208 {ECO:0000244|PDB:1EYE}.
HELIX 214 219 {ECO:0000244|PDB:1EYE}.
STRAND 223 225 {ECO:0000244|PDB:1EYE}.
HELIX 230 233 {ECO:0000244|PDB:1EYE}.
HELIX 234 246 {ECO:0000244|PDB:1EYE}.
STRAND 250 255 {ECO:0000244|PDB:1EYE}.
HELIX 257 271 {ECO:0000244|PDB:1EYE}.
SEQUENCE 280 AA; 28843 MW; 737AB6DF12C51C8C CRC64;
MSPAPVQVMG VLNVTDDSFS DGGCYLDLDD AVKHGLAMAA AGAGIVDVGG ESSRPGATRV
DPAVETSRVI PVVKELAAQG ITVSIDTMRA DVARAALQNG AQMVNDVSGG RADPAMGPLL
AEADVPWVLM HWRAVSADTP HVPVRYGNVV AEVRADLLAS VADAVAAGVD PARLVLDPGL
GFAKTAQHNW AILHALPELV ATGIPVLVGA SRKRFLGALL AGPDGVMRPT DGRDTATAVI
SALAALHGAW GVRVHDVRAS VDAIKVVEAW MGAERIERDG


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