ID A3TPK5_9MICO Unreviewed; 290 AA.
AC A3TPK5;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
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 ORFNames=JNB_15903 {ECO:0000313|EMBL:EAP98463.1};
OS Janibacter sp. HTCC2649.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=313589 {ECO:0000313|EMBL:EAP98463.1, ECO:0000313|Proteomes:UP000005063};
RN [1] {ECO:0000313|EMBL:EAP98463.1, ECO:0000313|Proteomes:UP000005063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2649 {ECO:0000313|EMBL:EAP98463.1,
RC ECO:0000313|Proteomes:UP000005063};
RX PubMed=21075932; DOI=10.1128/JB.01298-10;
RA Thrash J.C., Cho J.C., Bertagnolli A.D., Ferriera S., Johnson J.,
RA Vergin K.L., Giovannoni S.J.;
RT "Genome sequence of the Marine Janibacter Sp. Strain HTCC2649.";
RL J. Bacteriol. 193:584-585(2011).
CC -!- FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with
CC 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-
CC dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
CC {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; 7,8-
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAP98463.1}.
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DR EMBL; AAMN01000003; EAP98463.1; -; Genomic_DNA.
DR RefSeq; WP_009777468.1; NZ_CH672413.1.
DR AlphaFoldDB; A3TPK5; -.
DR STRING; 313589.JNB_15903; -.
DR eggNOG; COG0294; Bacteria.
DR HOGENOM; CLU_008023_0_0_11; -.
DR OrthoDB; 9811744at2; -.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000005063; Unassembled WGS sequence.
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; Dihydropteroate synthase-like; 1.
DR InterPro; IPR045031; DHP_synth-like.
DR InterPro; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
DR NCBIfam; TIGR01496; DHPS; 1.
DR PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1.
DR PANTHER; PTHR20941:SF8; INACTIVE DIHYDROPTEROATE SYNTHASE 2; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 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 {ECO:0000256|RuleBase:RU361205};
KW Magnesium {ECO:0000256|RuleBase:RU361205};
KW Metal-binding {ECO:0000256|RuleBase:RU361205};
KW Reference proteome {ECO:0000313|Proteomes:UP000005063};
KW Transferase {ECO:0000256|RuleBase:RU361205}.
FT DOMAIN 18..271
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 290 AA; 31443 MW; 83BBB24744C12AAB CRC64;
MTELRFRLGR GEFDARSRLV MAIVNRTPDS FYDKGSTWRE DAAFDRVREV VAQGADIVDI
GGIKAAPGVE IGADEEKGRV VDFVAAVRAE HPDLLISVDT WRASVGRAVL EAGADILNDA
WGGADPELVE VAAEFDAAVV CTHTGGVTPR TRPHRIEYDD VVESVVESLV AQADRAVSVG
VARERIVIDP AHDFGKNSWH SLEVTRRLDE LVALDWPLLV SLSNKDFVGE ALDLPVGERL
TGTLAATAIS AWHGAHIYRV HEVVETRQVL DMVSVISGDL PPARTARGLA
//
