ID A0A420V734_9ACTN Unreviewed; 286 AA.
AC A0A420V734;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
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:RKM97464.1};
GN ORFNames=DC095_007020 {ECO:0000313|EMBL:RNC75643.1}, SFRA_007580
GN {ECO:0000313|EMBL:RKM97464.1};
OS Streptomyces xinghaiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1038928 {ECO:0000313|EMBL:RKM97464.1, ECO:0000313|Proteomes:UP000028058};
RN [1] {ECO:0000313|EMBL:RKM97464.1, ECO:0000313|Proteomes:UP000028058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19609 {ECO:0000313|EMBL:RKM97464.1,
RC ECO:0000313|Proteomes:UP000028058};
RX PubMed=25477406;
RA Bekker O.B., Klimina K.M., Vatlin A.A., Zakharevich N.V., Kasianov A.S.,
RA Danilenko V.N.;
RT "Draft Genome Sequence of Streptomyces fradiae ATCC 19609, a Strain Highly
RT Sensitive to Antibiotics.";
RL Genome Announc. 2:0-0(2014).
RN [2] {ECO:0000313|EMBL:RKM97464.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 19609 {ECO:0000313|EMBL:RKM97464.1};
RA Danilenko V.N., Bekker O.B., Vatlin A.;
RT "Genome sequencing of Streptomyces fradiae ATCC 19609.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RNC75643.1, ECO:0000313|Proteomes:UP000245280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OlgR {ECO:0000313|EMBL:RNC75643.1,
RC ECO:0000313|Proteomes:UP000245280};
RA Danilenko V.N., Bekker O.B., Vatlin A.;
RT "Genome sequencing of Streptomyces xinghaiensis (fradiae) OlgR.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RKM97464.1}.
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DR EMBL; JNAD02000003; RKM97464.1; -; Genomic_DNA.
DR EMBL; QFBD02000002; RNC75643.1; -; Genomic_DNA.
DR RefSeq; WP_043473631.1; NZ_QFBD02000002.1.
DR AlphaFoldDB; A0A420V734; -.
DR OrthoDB; 9811744at2; -.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000028058; Unassembled WGS sequence.
DR Proteomes; UP000245280; 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:UP000028058};
KW Transferase {ECO:0000256|RuleBase:RU361205, ECO:0000313|EMBL:RKM97464.1}.
FT DOMAIN 14..267
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 286 AA; 30828 MW; 95B44B10D2046B7A CRC64;
MLRLGKREFG EHEPVVMAIV NRTPDSFYDQ GSTFRDEPAL ARVGQAIAEG AAIVDIGGVK
AGPGEEVTAE EEARRTVGFV AEVRRRHPEV VISVDTWRHE VAEAVCEAGA DLLNDAWGGV
DPQLAAVAAR YGAGLVCTHA GGAEPRTRPH RVAYEDVMAD ILRVTQGLAE RAVELGVRRD
GILIDPGHDF GKNTRHSLEA TRRLGEMTAT GWPVLVSLSN KDFVGETLDR PVKQRLTGTL
AATAVSAWLG ARVYRVHEVA ETRQVLDMVA SIAGHRPPAV ARRGLA
//
