Legends: 1, Magnesium. {ECO:0000250|UniProtKB:P9WND1}; 2, BINDING 6-hydroxymethyl-7,8-dihydropterin diphosphate. {ECO:0000250|UniProtKB:P0AC13}; 3, REGION 6-hydroxymethyl-7,8-dihydropterin diphosphate binding. {ECO:0000250|UniProtKB:P0AC13}; 4, ipat:DHPS_1 [T]; 5, ipat:DHPS_2 [T].
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ID DHP1_CORGT Reviewed; 279 AA.
AC P0C004; P11744; Q93K51;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 30-NOV-2016, entry version 55.
DE RecName: Full=Dihydropteroate synthase type-1;
DE EC=2.5.1.15;
DE AltName: Full=Dihydropteroate pyrophosphorylase type I;
DE AltName: Full=Dihydropteroate synthase type I;
DE Short=DHPS;
GN Name=sulI;
OS Corynebacterium glutamicum (Brevibacterium saccharolyticum).
OG Plasmid pCG4.
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=1718;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31830 / T250; PLASMID=pCG4;
RX PubMed=9868786; DOI=10.1111/j.1574-6968.1998.tb13345.x;
RA Nesvera J., Hochmannova J., Patek M.;
RT "An integron of class 1 is present on the plasmid pCG4 from Gram-
RT positive bacterium Corynebacterium glutamicum.";
RL FEMS Microbiol. Lett. 169:391-395(1998).
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:0000250|UniProtKB:P0AC13}.
CC -!- CATALYTIC ACTIVITY: 6-hydroxymethyl-7,8-dihydropterin diphosphate
CC + 4-aminobenzoate = diphosphate + dihydropteroate.
CC {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;
CC 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
CC -!- SUBUNIT: Homodimer or homotrimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: The sulI gene is located on various large self-
CC transmissible resistance plasmids and on transposons related to
CC Tn21.
CC -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 pterin-binding domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00334}.
DR EMBL; Y14748; CAA75045.1; -; Genomic_DNA.
DR RefSeq; NP_478074.1; NC_003227.1.
DR RefSeq; NP_862308.1; NC_004945.1.
DR RefSeq; WP_000259031.1; NC_004945.1.
DR ProteinModelPortal; P0C004; -.
DR GeneID; 1132010; -.
DR GeneID; 1450507; -.
DR GeneID; 4999104; -.
DR UniPathway; UPA00077; UER00156.
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;
KW Folate biosynthesis; Magnesium; Metal-binding; Plasmid; Transferase;
KW Transposable element.
FT CHAIN 1 279 Dihydropteroate synthase type-1.
FT /FTId=PRO_0000168200.
FT DOMAIN 1 258 Pterin-binding. {ECO:0000255|PROSITE-
FT ProRule:PRU00334}.
FT REGION 246 248 6-hydroxymethyl-7,8-dihydropterin
FT diphosphate binding.
FT {ECO:0000250|UniProtKB:P0AC13}.
FT METAL 9 9 Magnesium.
FT {ECO:0000250|UniProtKB:P9WND1}.
FT BINDING 82 82 6-hydroxymethyl-7,8-dihydropterin
FT diphosphate.
FT {ECO:0000250|UniProtKB:P0AC13}.
FT BINDING 101 101 6-hydroxymethyl-7,8-dihydropterin
FT diphosphate.
FT {ECO:0000250|UniProtKB:P0AC13}.
FT BINDING 173 173 6-hydroxymethyl-7,8-dihydropterin
FT diphosphate.
FT {ECO:0000250|UniProtKB:P0AC13}.
FT BINDING 212 212 6-hydroxymethyl-7,8-dihydropterin
FT diphosphate.
FT {ECO:0000250|UniProtKB:P0AC13}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 4 19 ipat:DHPS_1 [T]
FT MYHIT 2 258 iprf:PTERIN_BINDING [T]
FT MYHIT 38 51 ipat:DHPS_2 [T]
FT MYHIT 5 248 ipfam:Pterin_bind [T]
SQ SEQUENCE 279 AA; 30126 MW; 13EE36C6E3FBDF63 CRC64;
MVTVFGILNL TEDSFFDESR RLDPAGAVTA AIEMLRVGSD VVDVGPAASH PDARPVSPAD
EIRRIAPLLD ALSDQMHRVS IDSFQPETQR YALKRGVGYL NDIQGFPDPA LYPDIAEADC
RLVVMHSAQR DGIATRTGHL RPEDALDEIV RFFEARVSAL RRSGVAADRL ILDPGMGFFL
SPAPETSLHV LSNLQKLKSA LGLPLLVSVS RKSFLGATVG LPVKDLGPAS LAAELHAIGN
GADYVRTHAP GDLRSAITFS ETLAKFRSRD ARDRGLDHA
//
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