(data stored in ACNUC7421 zone)

SWISSPROT: A8LCJ6_FRASN

ID   A8LCJ6_FRASN            Unreviewed;       304 AA.
AC   A8LCJ6;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 67.
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=Franean1_0168 {ECO:0000313|EMBL:ABW09635.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09635.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CP000820; ABW09635.1; -; Genomic_DNA.
DR   RefSeq; WP_012157612.1; NC_009921.1.
DR   STRING; 298653.Franean1_0168; -.
DR   EnsemblBacteria; ABW09635; ABW09635; Franean1_0168.
DR   KEGG; fre:Franean1_0168; -.
DR   eggNOG; ENOG4105EEI; Bacteria.
DR   eggNOG; COG0294; LUCA.
DR   HOGENOM; HOG000217509; -.
DR   KO; K00796; -.
DR   OMA; WAVRVHD; -.
DR   OrthoDB; 1275854at2; -.
DR   BioCyc; FSP298653:G1G9X-166-MONOMER; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000001313; 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; A8LCJ6.
DR   SWISS-2DPAGE; A8LCJ6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001313};
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:UP000001313};
KW   Transferase {ECO:0000256|RuleBase:RU361205,
KW   ECO:0000313|EMBL:ABW09635.1}.
FT   DOMAIN       15    272       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
SQ   SEQUENCE   304 AA;  31010 MW;  71456E4059545EF1 CRC64;
     MTGPRDDLFA PDAPTRVMGV VNVTPDSFSD GGAYPDPHDA VRAAQLMIEQ GADVIDVGGE
     STRPGAPRVV ASEELRRVLP VVAQLASAGV PVSVDTSRAS VASAAVDAGA LLVNDVSCGR
     NAELLRIVAD RGVHYVLMHS RGSSTDMAAH AVYNDVVTDV VGELAARLDV VLAAGVAEDK
     VIIDPGIGFA KTPAHNWALL ANLGAVASLG RPLLVGTSRK SFLGAAVSGP GELPRPADER
     DDATQATTAL LADAGVWAVR VHAVRPAVDA VRVVRAWQQA ARASGAGRPR AAVSGSAPAA
     GPSR
//

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