(data stored in SCRATCH zone)

SWISSPROT: DHPS_BACSU

ID   DHPS_BACSU              Reviewed;         285 AA.
AC   P28822;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   04-AUG-2003, sequence version 2.
DT   11-DEC-2019, entry version 131.
DE   RecName: Full=Dihydropteroate synthase;
DE            Short=DHPS;
DE            EC=2.5.1.15;
DE   AltName: Full=Dihydropteroate pyrophosphorylase;
GN   Name=sul; OrderedLocusNames=BSU00770;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ASB342;
RX   PubMed=2123867; DOI=10.1128/jb.172.12.7211-7226.1990;
RA   Slock J., Stahly D.P., Han C.-Y., Six E.W., Crawford I.P.;
RT   "An apparent Bacillus subtilis folic acid biosynthetic operon containing
RT   pab, an amphibolic trpG gene, a third gene required for synthesis of para-
RT   aminobenzoic acid, and the dihydropteroate synthase gene.";
RL   J. Bacteriol. 172:7211-7226(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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:0000250|UniProtKB:P0AC13}.
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:0000250|UniProtKB:P0AC13};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0AC13};
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   -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
DR   EMBL; M34053; AAA22697.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05312.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11853.1; -; Genomic_DNA.
DR   PIR; G69719; G69719.
DR   RefSeq; NP_387958.1; NC_000964.3.
DR   RefSeq; WP_003242672.1; NZ_JNCM01000028.1.
DR   SMR; P28822; -.
DR   STRING; 224308.BSU00770; -.
DR   PaxDb; P28822; -.
DR   PRIDE; P28822; -.
DR   EnsemblBacteria; CAB11853; CAB11853; BSU00770.
DR   GeneID; 936256; -.
DR   KEGG; bsu:BSU00770; -.
DR   PATRIC; fig|224308.179.peg.77; -.
DR   eggNOG; ENOG4105EEI; Bacteria.
DR   eggNOG; COG0294; LUCA.
DR   HOGENOM; HOG000217509; -.
DR   InParanoid; P28822; -.
DR   KO; K00796; -.
DR   OMA; VGASRKN; -.
DR   PhylomeDB; P28822; -.
DR   BioCyc; BSUB:BSU00770-MONOMER; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004156; F:dihydropteroate synthase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   CDD; cd00739; DHPS; 1.
DR   Gene3D; 3.20.20.20; -; 1.
DR   InterPro; IPR006390; DHP_synth.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   SUPFAM; SSF51717; SSF51717; 1.
DR   TIGRFAMs; TIGR01496; DHPS; 1.
DR   PROSITE; PS00792; DHPS_1; 1.
DR   PROSITE; PS00793; DHPS_2; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   3: Inferred from homology;
DR   PRODOM; P28822.
DR   SWISS-2DPAGE; P28822.
KW   Folate biosynthesis; Magnesium; Metal-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..285
FT                   /note="Dihydropteroate synthase"
FT                   /id="PRO_0000168205"
FT   DOMAIN          25..271
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT   REGION          259..261
FT                   /note="6-hydroxymethyl-7,8-dihydropterin diphosphate
FT                   binding"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   METAL           32
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250|UniProtKB:P9WND1"
FT   BINDING         72
FT                   /note="6-hydroxymethyl-7,8-dihydropterin diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         106
FT                   /note="6-hydroxymethyl-7,8-dihydropterin diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         125
FT                   /note="6-hydroxymethyl-7,8-dihydropterin diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         189
FT                   /note="6-hydroxymethyl-7,8-dihydropterin diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         225
FT                   /note="6-hydroxymethyl-7,8-dihydropterin diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   CONFLICT        195
FT                   /note="A -> P (in Ref. 1; AAA22697)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   285 AA;  31002 MW;  F2878DEC3D9000D6 CRC64;
     MAQHTIDQTQ VIHTKPSALS YKEKTLVMGI LNVTPDSFSD GGKYDSLDKA LLHAKEMIDD
     GAHIIDIGGE STRPGAECVS EDEEMSRVIP VIERITKELG VPISVDTYKA SVADEAVKAG
     ASIINDIWGA KHDPKMASVA AEHNVPIVLM HNRPERNYND LLPDMLSDLM ESVKIAVEAG
     VDEKNIILDP GIGFAKTYHD NLAVMNKLEI FSGLGYPVLL ATSRKRFIGR VLDLPPEERA
     EGTGATVCLG IQKGCDIVRV HDVKQIARMA KMMDAMLNKG GVHHG
//

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