(data stored in SCRATCH zone)

SWISSPROT: Q9FBL7_STRCO

ID   Q9FBL7_STRCO            Unreviewed;       294 AA.
AC   Q9FBL7;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   08-MAY-2019, entry version 102.
DE   RecName: Full=Dihydropteroate synthase {ECO:0000256|RuleBase:RU361205};
DE            Short=DHPS {ECO:0000256|RuleBase:RU361205};
DE            EC=2.5.1.15 {ECO:0000256|RuleBase:RU361205};
DE   AltName: Full=Dihydropteroate pyrophosphorylase {ECO:0000256|RuleBase:RU361205};
GN   OrderedLocusNames=SCO5141 {ECO:0000313|EMBL:CAC01342.1};
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226 {ECO:0000313|Proteomes:UP000001973};
RN   [1] {ECO:0000313|EMBL:CAC01342.1, ECO:0000313|Proteomes:UP000001973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145
RC   {ECO:0000313|Proteomes:UP000001973};
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.H., Kieser T., Larke L., Murphy L., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA)
CC       with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to
CC       form 7,8-dihydropteroate (H2Pte), the immediate precursor of
CC       folate derivatives. {ECO:0000256|RuleBase:RU361205}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361205};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
CC       7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC       dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
CC       {ECO:0000256|RuleBase:RU361205}.
CC   -!- SIMILARITY: Belongs to the DHPS family.
CC       {ECO:0000256|RuleBase:RU361205}.
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DR   EMBL; AL939122; CAC01342.1; -; Genomic_DNA.
DR   RefSeq; NP_629289.1; NC_003888.3.
DR   RefSeq; WP_011030080.1; NC_003888.3.
DR   STRING; 100226.SCO5141; -.
DR   EnsemblBacteria; CAC01342; CAC01342; CAC01342.
DR   GeneID; 1100582; -.
DR   KEGG; sco:SCO5141; -.
DR   PATRIC; fig|100226.15.peg.5224; -.
DR   eggNOG; ENOG4105EEI; Bacteria.
DR   eggNOG; COG0294; LUCA.
DR   HOGENOM; HOG000217509; -.
DR   InParanoid; Q9FBL7; -.
DR   KO; K00796; -.
DR   OMA; DPGHDFG; -.
DR   PhylomeDB; Q9FBL7; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; -; 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; Q9FBL7.
DR   SWISS-2DPAGE; Q9FBL7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001973};
KW   Folate biosynthesis {ECO:0000256|RuleBase:RU361205};
KW   Magnesium {ECO:0000256|RuleBase:RU361205};
KW   Metal-binding {ECO:0000256|RuleBase:RU361205};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001973};
KW   Transferase {ECO:0000256|RuleBase:RU361205}.
FT   DOMAIN       22    275       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
SQ   SEQUENCE   294 AA;  31675 MW;  62BE9D5756CA007A CRC64;
     MDQEMSQGML RLGRREFAAH EPVIMAIVNR TPDSFYDRGA TFGDEPALAR VEQAVAEGAA
     IIDVGGVKAG PGDEVSAAEE ARRTVGFVAE VRRRHPDVVI SVDTWRHEVG EAVCEAGADL
     LNDAWGGVDP KLAEVAARYG VGLVCTHAGG AEPRTRPHRV TYDDVVADVL RVTLGLAERA
     VGLGVPRESV LIDPGHDFGK NTRHSLEATR RLGEMVETGW PVLVSLSNKD FVGETLDRPV
     KERLIGTLAT TAVSAWLGAR VYRVHEVAET RQVLDMVATI AGHREPAVAR RGLA
//

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