ID A0A0A0HHV9_9RHOB Unreviewed; 315 AA.
AC A0A0A0HHV9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458, ECO:0000256|RuleBase:RU361205};
DE Short=DHPS {ECO:0000256|RuleBase:RU361205};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458, ECO:0000256|RuleBase:RU361205};
DE AltName: Full=Dihydropteroate pyrophosphorylase {ECO:0000256|RuleBase:RU361205};
GN ORFNames=rosmuc_02839 {ECO:0000313|EMBL:KGM86551.1};
OS Roseovarius mucosus DSM 17069.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1288298 {ECO:0000313|EMBL:KGM86551.1, ECO:0000313|Proteomes:UP000030021};
RN [1] {ECO:0000313|EMBL:KGM86551.1, ECO:0000313|Proteomes:UP000030021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17069 {ECO:0000313|EMBL:KGM86551.1,
RC ECO:0000313|Proteomes:UP000030021};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (JAN-2013) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate =
CC 7,8-dihydropteroate + diphosphate; Xref=Rhea:RHEA:19949,
CC ChEBI:CHEBI:17836, ChEBI:CHEBI:17839, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:72950; EC=2.5.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00000012};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC 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|ARBA:ARBA00004763, 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:KGM86551.1}.
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DR EMBL; AONH01000016; KGM86551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0HHV9; -.
DR STRING; 215743.ROSMUCSMR3_03373; -.
DR PATRIC; fig|1288298.3.peg.2857; -.
DR eggNOG; COG0294; Bacteria.
DR HOGENOM; CLU_008023_0_1_5; -.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000030021; 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:SF1; FOLIC ACID SYNTHESIS PROTEIN FOL1; 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|ARBA:ARBA00022909,
KW ECO:0000256|RuleBase:RU361205};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU361205};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361205};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361205}.
FT DOMAIN 71..315
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 315 AA; 33146 MW; 209F4CF78305E490 CRC64;
MPYYRPIPRT DPARPAGALT LAGGLCWFDT VEVLDRSAPS YLMPAADLPT EALHRLTTPR
APVAGLDMAA PQIMGILNVT PDSFSDGGQH FDPEVALAHA RQMAADGAAI LDVGGESTRP
GAAPVPIEDE IARTAPVIAA LRAGITTPIS IDTRKTPVAQ AAHAAGANLI NDVAGFTYDP
ALAPYAATHA LPVCVMHAQG TPETMQQDPR YDHVLLDVYD WLAARIEALV ALGIPRARIV
TDPGIGFGKT VAHNLTLLQN LSLFHSLGCP ILLGASRKRF IGEISRTPVA ADRIPRLARR
GLGRRGAGGA DPARA
//
