ID M2XXF8_9MICC Unreviewed; 305 AA.
AC M2XXF8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=C884_01544 {ECO:0000313|EMBL:EME37493.1};
OS Kocuria palustris PEL.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1236550 {ECO:0000313|EMBL:EME37493.1, ECO:0000313|Proteomes:UP000009877};
RN [1] {ECO:0000313|EMBL:EME37493.1, ECO:0000313|Proteomes:UP000009877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEL {ECO:0000313|EMBL:EME37493.1,
RC ECO:0000313|Proteomes:UP000009877};
RX PubMed=24504000;
RA Sharma G., Khatri I., Subramanian S.;
RT "Draft Genome Sequence of Kocuria palustris PEL.";
RL Genome Announc. 2:e01261-13(2014).
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:EME37493.1}.
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DR EMBL; ANHZ02000003; EME37493.1; -; Genomic_DNA.
DR AlphaFoldDB; M2XXF8; -.
DR STRING; 71999.KPaMU14_01555; -.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000009877; 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 Reference proteome {ECO:0000313|Proteomes:UP000009877};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361205}.
FT DOMAIN 33..290
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 305 AA; 32221 MW; 5EA567381C9E19CE CRC64;
MQPTPPEAVA PQPAAVRREL GWGDWAGLPS GRTLVMGILN VTPDSFSDGG RHDSHRAAIA
HGHELASQGA DLIDVGGEST RPGSQRVDPE EERRRILPVI RELSDAGIVL SVDTFNPSTA
EAALDAGAHC VNDVSGVAVR DGMVPLVAER QAPYICMHSR GTPGTMDSLA VYDDLVGDVL
REIHEVAQRF LDAGLDPSKL VLDPGLGFAK GGRQDWQLLE ALPRFVATGY PILVAASRKR
FIGHLLGNGT EPRPADQRDI ATAAISALSA DRGAWAVRVH DVASSVDALA VAGAWNRPVG
KEGIA
//
