ID F3NMM9_9ACTN Unreviewed; 286 AA.
AC F3NMM9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=SGM_4393 {ECO:0000313|EMBL:EGG45065.1};
OS Streptomyces griseoaurantiacus M045.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG45065.1, ECO:0000313|Proteomes:UP000003022};
RN [1] {ECO:0000313|EMBL:EGG45065.1, ECO:0000313|Proteomes:UP000003022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M045 {ECO:0000313|EMBL:EGG45065.1,
RC ECO:0000313|Proteomes:UP000003022};
RX PubMed=21551298; DOI=10.1128/JB.05053-11;
RA Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT "Draft genome sequence of the marine bacterium Streptomyces
RT griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT with a pABA core component.";
RL J. Bacteriol. 193:3417-3418(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:EGG45065.1}.
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DR EMBL; AEYX01000041; EGG45065.1; -; Genomic_DNA.
DR RefSeq; WP_006142205.1; NZ_AEYX01000041.1.
DR AlphaFoldDB; F3NMM9; -.
DR STRING; 996637.SGM_4393; -.
DR eggNOG; COG0294; Bacteria.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000003022; 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:UP000003022};
KW Transferase {ECO:0000256|RuleBase:RU361205}.
FT DOMAIN 14..267
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 286 AA; 30730 MW; B3EF97CA1926725B CRC64;
MLRLGGREFG EHEPVIMAIV NRTPDSFYDQ GATFHDEPAL ARVERAVSEG AAIVDIGGVK
AGPGEEVTAE EEARRTVGFV AEVRRRFPDV IISVDTWRAE VGEAVCEAGA DLLNDAWGGV
DPGLAEVAAR YGVGLVCTHA GGAEPRTRPH RVTYEDVMAD ILRVTLGLAE RAVSLGVPRE
SVLIDPGHDF GKNTRHSLEA TRRLEEMVET GWPVLVSLSN KDFVGETLDR PVKERLVGTL
ATTAVSAWLG AQVYRVHEVA ETRQVLGMVS AIAGHGQPAV ARRGLA
//
