(data stored in ACNUC1104 zone)

SWISSPROT: D3UYY5_XENBS

ID   D3UYY5_XENBS            Unreviewed;       285 AA.
AC   D3UYY5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 51.
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   Name=folP {ECO:0000313|EMBL:CBJ79513.1};
GN   OrderedLocusNames=XBJ1_0363 {ECO:0000313|EMBL:CBJ79513.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79513.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79513.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79513.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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; FN667741; CBJ79513.1; -; Genomic_DNA.
DR   RefSeq; WP_012986972.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0363; -.
DR   EnsemblBacteria; CBJ79513; CBJ79513; XBJ1_0363.
DR   GeneID; 8829987; -.
DR   KEGG; xbo:XBJ1_0363; -.
DR   PATRIC; fig|406818.4.peg.333; -.
DR   eggNOG; ENOG4105EEI; Bacteria.
DR   eggNOG; COG0294; LUCA.
DR   HOGENOM; HOG000217510; -.
DR   KO; K00796; -.
DR   OMA; WAVRVHD; -.
DR   BioCyc; XBOV406818:XBJ1_RS01585-MONOMER; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000002045; 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; D3UYY5.
DR   SWISS-2DPAGE; D3UYY5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
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:UP000002045};
KW   Transferase {ECO:0000256|RuleBase:RU361205,
KW   ECO:0000313|EMBL:CBJ79513.1}.
FT   DOMAIN       15    267       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
SQ   SEQUENCE   285 AA;  30807 MW;  DBEA918288BF5C62 CRC64;
     MKLTARGSVL DLSRPQVMGI LNVTPDSFSD GGNHSTFDAA LRHAATMIEE GAAIIDVGGE
     STRPGAVDVS EQEELDRVVP VVEALARRFD AWISIDTSKA IVMQESAKVG AHMINDIRSL
     QEFGALDAAV KTGLPVCLMH MQGQPSTMQA EPYYEDAVWE TKTFLTRQID RCVAAGIAKN
     KLILDPGFGF GKNLSHNYQL LAHLEEFHHL GLPILAGMSR KSMIGQLLHV PPQECVTGSI
     ACAVIAAMQG AQIIRVHDVK ETVQTMQIVQ ATLSAKNILA VKNTL
//

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