(data stored in ACNUC7421 zone)

SWISSPROT: D6XV65_BACIE

ID   D6XV65_BACIE            Unreviewed;       286 AA.
AC   D6XV65;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 58.
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=Bsel_0073 {ECO:0000313|EMBL:ADH97623.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97623.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97623.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001791; ADH97623.1; -; Genomic_DNA.
DR   RefSeq; WP_013171053.1; NC_014219.1.
DR   STRING; 439292.Bsel_0073; -.
DR   EnsemblBacteria; ADH97623; ADH97623; Bsel_0073.
DR   KEGG; bse:Bsel_0073; -.
DR   eggNOG; ENOG4105EEI; Bacteria.
DR   eggNOG; COG0294; LUCA.
DR   HOGENOM; HOG000217509; -.
DR   KO; K00796; -.
DR   OMA; WAVRVHD; -.
DR   OrthoDB; 1275854at2; -.
DR   BioCyc; BSEL439292:G1GLR-80-MONOMER; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000000271; 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; -; 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; D6XV65.
DR   SWISS-2DPAGE; D6XV65.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
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:UP000000271};
KW   Transferase {ECO:0000256|RuleBase:RU361205,
KW   ECO:0000313|EMBL:ADH97623.1}.
FT   DOMAIN       22    268       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
SQ   SEQUENCE   286 AA;  31830 MW;  3D37EE07653EC423 CRC64;
     MMKEYFSTMK WDRYELNFAD KTLIMGILNV TPDSFSDGGK FQSEQEWQDR AKEMVRQGAD
     IIDIGGESTR PGSTPVPADE ELGRVIPAIR AIRSVVDVPI SIDTYKSDVA EAAIQAGASI
     INDVWGARYD SGMAEVAARF DVPIILMHNR ERMDYTDLIT DMKEDLRKSV RIAKEAGVKD
     ERIILDPGIG FAKTYEDNLT VMRELDAFMD LGYPMLLGTS RKSLIAKTLN LPVHERVEGT
     GATVCLGIEK GCDIVRVHDV LEMSRMARMM DVMIGKSQVP LEKSGA
//

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