ID Q81VW8_BACAN Unreviewed; 280 AA.
AC Q81VW8; A0A2B6BWX3; E9QTW3; E9QTW4; E9QTW5; Q2QCA4; Q6I4X2; Q6KYL6;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 173.
DE RecName: Full=Dihydropteroate synthase {ECO:0000256|ARBA:ARBA00016919, ECO:0000256|RuleBase:RU361205};
DE Short=DHPS {ECO:0000256|RuleBase:RU361205};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458, ECO:0000256|RuleBase:RU361205};
DE AltName: Full=Dihydropteroate pyrophosphorylase {ECO:0000256|ARBA:ARBA00030193, ECO:0000256|RuleBase:RU361205};
GN Name=folP {ECO:0000313|EMBL:AAZ65853.1};
GN OrderedLocusNames=GBAA_0071 {ECO:0000313|EMBL:AAT29149.1};
OS Bacillus anthracis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392 {ECO:0000313|EMBL:AAZ65853.1};
RN [1] {ECO:0007829|PDB:1TWS, ECO:0007829|PDB:1TWW}
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 5-280.
RX PubMed=15341734; DOI=10.1016/j.str.2004.07.011;
RA Babaoglu K., Qi J., Lee R.E., White S.W.;
RT "Crystal structure of 7,8-dihydropteroate synthase from Bacillus anthracis:
RT mechanism and novel inhibitor design.";
RL Structure 12:1705-1717(2004).
RN [2] {ECO:0000313|EMBL:AAZ65853.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Sterne {ECO:0000313|EMBL:AAZ65853.1};
RX PubMed=17536929; DOI=10.1089/mdr.2006.9992;
RA Valderas M.W., Bourne P.C., Barrow W.W.;
RT "Genetic basis for sulfonamide resistance in Bacillus anthracis.";
RL Microb. Drug Resist. 13:11-20(2007).
RN [3] {ECO:0000313|EMBL:AAT29149.1, ECO:0000313|Proteomes:UP000000594}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor {ECO:0000313|Proteomes:UP000000594}, and Ames
RC Ancestor {ECO:0000313|EMBL:AAT29149.1};
RX PubMed=18952800; DOI=10.1128/JB.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [4] {ECO:0007829|PDB:3H21, ECO:0007829|PDB:3H22}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 5-280.
RX PubMed=19899766; DOI=10.1021/jm900861d;
RA Hevener K.E., Yun M.K., Qi J., Kerr I.D., Babaoglu K., Hurdle J.G.,
RA Balakrishna K., White S.W., Lee R.E.;
RT "Structural studies of pterin-based inhibitors of dihydropteroate
RT synthase.";
RL J. Med. Chem. 53:166-177(2010).
RN [5] {ECO:0007829|PDB:4D8A, ECO:0007829|PDB:4D8Z}
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 5-280.
RX PubMed=22416048; DOI=10.1002/cmdc.201200049;
RA Zhao Y., Hammoudeh D., Yun M.K., Qi J., White S.W., Lee R.E.;
RT "Structure-based design of novel pyrimido[4,5-c]pyridazine derivatives as
RT dihydropteroate synthase inhibitors with increased affinity.";
RL ChemMedChem 7:861-870(2012).
RN [6] {ECO:0007829|PDB:3TYA, ECO:0007829|PDB:3TYB}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 5-280.
RX PubMed=22383850; DOI=10.1126/science.1214641;
RA Yun M.K., Wu Y., Li Z., Zhao Y., Waddell M.B., Ferreira A.M., Lee R.E.,
RA Bashford D., White S.W.;
RT "Catalysis and sulfa drug resistance in dihydropteroate synthase.";
RL Science 335:1110-1114(2012).
RN [7] {ECO:0007829|PDB:4NHV, ECO:0007829|PDB:4NIL}
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 5-280.
RX PubMed=24650357; DOI=10.1021/cb500038g;
RA Hammoudeh D.I., Date M., Yun M.K., Zhang W., Boyd V.A., Viacava Follis A.,
RA Griffith E., Lee R.E., Bashford D., White S.W.;
RT "Identification and characterization of an allosteric inhibitory site on
RT dihydropteroate synthase.";
RL ACS Chem. Biol. 9:1294-1302(2014).
CC -!- FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with
CC 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-
CC dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
CC {ECO:0000256|RuleBase:RU361205}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate =
CC 7,8-dihydropteroate + diphosphate; Xref=Rhea:RHEA:19949,
CC ChEBI:CHEBI:17836, ChEBI:CHEBI:17839, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:72950; EC=2.5.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00000012};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU361205};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-
CC dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004763, ECO:0000256|RuleBase:RU361205}.
CC -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000256|ARBA:ARBA00009503,
CC ECO:0000256|RuleBase:RU361205}.
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DR EMBL; AE017334; AAT29149.1; -; Genomic_DNA.
DR EMBL; DQ139876; AAZ65853.1; -; Genomic_DNA.
DR PDB; 1TWS; X-ray; 2.00 A; A/B=4-280.
DR PDB; 1TWW; X-ray; 2.50 A; A/B=4-280.
DR PDB; 1TWZ; X-ray; 2.75 A; A/B=4-280.
DR PDB; 1TX0; X-ray; 2.15 A; A/B=4-280.
DR PDB; 1TX2; X-ray; 1.83 A; A/B=4-280.
DR PDB; 3H21; X-ray; 2.32 A; A/B=4-280.
DR PDB; 3H22; X-ray; 2.40 A; A/B=4-280.
DR PDB; 3H23; X-ray; 2.20 A; A/B=4-280.
DR PDB; 3H24; X-ray; 2.50 A; A/B=4-280.
DR PDB; 3H26; X-ray; 2.50 A; A/B=4-280.
DR PDB; 3H2A; X-ray; 2.40 A; A/B=4-280.
DR PDB; 3H2C; X-ray; 2.60 A; A/B=4-280.
DR PDB; 3H2E; X-ray; 2.00 A; A/B=4-280.
DR PDB; 3H2F; X-ray; 2.20 A; A/B=4-280.
DR PDB; 3H2M; X-ray; 2.31 A; A/B=4-280.
DR PDB; 3H2N; X-ray; 2.40 A; A/B=4-280.
DR PDB; 3H2O; X-ray; 2.70 A; A/B=4-280.
DR PDB; 3TYA; X-ray; 2.61 A; A/B=5-280.
DR PDB; 3TYB; X-ray; 2.60 A; A/B=5-280.
DR PDB; 3TYC; X-ray; 2.30 A; A/B=5-280.
DR PDB; 3TYD; X-ray; 2.50 A; A/B=5-280.
DR PDB; 3TYE; X-ray; 2.30 A; A/B=5-280.
DR PDB; 4D8A; X-ray; 2.18 A; A/B=4-280.
DR PDB; 4D8Z; X-ray; 2.20 A; A/B=4-280.
DR PDB; 4D9P; X-ray; 2.26 A; A/B=4-280.
DR PDB; 4DAF; X-ray; 2.50 A; A/B=4-280.
DR PDB; 4DAI; X-ray; 2.50 A; A/B=4-280.
DR PDB; 4DB7; X-ray; 2.50 A; A/B=4-280.
DR PDB; 4NHV; X-ray; 1.99 A; A/B=5-280.
DR PDB; 4NIL; X-ray; 2.18 A; A/B=5-280.
DR PDB; 4NIR; X-ray; 1.77 A; A/B=5-280.
DR PDB; 4NL1; X-ray; 2.30 A; A/B=5-280.
DR PDBsum; 1TWS; -.
DR PDBsum; 1TWW; -.
DR PDBsum; 1TWZ; -.
DR PDBsum; 1TX0; -.
DR PDBsum; 1TX2; -.
DR PDBsum; 3H21; -.
DR PDBsum; 3H22; -.
DR PDBsum; 3H23; -.
DR PDBsum; 3H24; -.
DR PDBsum; 3H26; -.
DR PDBsum; 3H2A; -.
DR PDBsum; 3H2C; -.
DR PDBsum; 3H2E; -.
DR PDBsum; 3H2F; -.
DR PDBsum; 3H2M; -.
DR PDBsum; 3H2N; -.
DR PDBsum; 3H2O; -.
DR PDBsum; 3TYA; -.
DR PDBsum; 3TYB; -.
DR PDBsum; 3TYC; -.
DR PDBsum; 3TYD; -.
DR PDBsum; 3TYE; -.
DR PDBsum; 4D8A; -.
DR PDBsum; 4D8Z; -.
DR PDBsum; 4D9P; -.
DR PDBsum; 4DAF; -.
DR PDBsum; 4DAI; -.
DR PDBsum; 4DB7; -.
DR PDBsum; 4NHV; -.
DR PDBsum; 4NIL; -.
DR PDBsum; 4NIR; -.
DR PDBsum; 4NL1; -.
DR AlphaFoldDB; Q81VW8; -.
DR SMR; Q81VW8; -.
DR BindingDB; Q81VW8; -.
DR ChEMBL; CHEMBL1075045; -.
DR DrugBank; DB04047; 6-hydroxymethylpterin diphosphate.
DR DrugBank; DB03705; 6-Methylamino-5-Nitroisocytosine.
DR DrugBank; DB03592; Pterin-6-Yl-Methyl-Monophosphate.
DR DrugBank; DB04196; Pteroic acid.
DR DNASU; 1083704; -.
DR KEGG; bar:GBAA_0071; -.
DR PATRIC; fig|1392.236.peg.73; -.
DR HOGENOM; CLU_008023_0_2_9; -.
DR OMA; FATPRDC; -.
DR BRENDA; 2.5.1.15; 634.
DR UniPathway; UPA00077; UER00156.
DR EvolutionaryTrace; Q81VW8; -.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00739; DHPS; 1.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR InterPro; IPR045031; DHP_synth-like.
DR InterPro; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
DR NCBIfam; TIGR01496; DHPS; 1.
DR PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1.
DR PANTHER; PTHR20941:SF1; FOLIC ACID SYNTHESIS PROTEIN FOL1; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR PROSITE; PS00792; DHPS_1; 1.
DR PROSITE; PS00793; DHPS_2; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1TWS, ECO:0007829|PDB:1TWW};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909,
KW ECO:0000256|RuleBase:RU361205};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU361205};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361205};
KW Reference proteome {ECO:0000313|Proteomes:UP000000594};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361205}.
FT DOMAIN 23..269
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 280 AA; 30976 MW; ACEB54F50658A69B CRC64;
MCSLKWDYDL RCGEYTLNLN EKTLIMGILN VTPDSFSDGG SYNEVDAAVR HAKEMRDEGA
HIIDIGGEST RPGFAKVSVE EEIKRVVPMI QAVSKEVKLP ISIDTYKAEV AKQAIEAGAH
IINDIWGAKA EPKIAEVAAH YDVPIILMHN RDNMNYRNLM ADMIADLYDS IKIAKDAGVR
DENIILDPGI GFAKTPEQNL EAMRNLEQLN VLGYPVLLGT SRKSFIGHVL DLPVEERLEG
TGATVCLGIE KGCEFVRVHD VKEMSRMAKM MDAMIGKGVK
//
