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Database: UniProt
Entry: A0A095YGA2_9ACTO
LinkDB: A0A095YGA2_9ACTO
Original site: A0A095YGA2_9ACTO 
ID   A0A095YGA2_9ACTO        Unreviewed;       267 AA.
AC   A0A095YGA2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=HMPREF1631_04685 {ECO:0000313|EMBL:KGF05582.1};
OS   Arcanobacterium sp. S3PF19.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Arcanobacterium.
OX   NCBI_TaxID=1219585 {ECO:0000313|EMBL:KGF05582.1, ECO:0000313|Proteomes:UP000054502};
RN   [1] {ECO:0000313|EMBL:KGF05582.1, ECO:0000313|Proteomes:UP000054502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S3PF19 {ECO:0000313|EMBL:KGF05582.1,
RC   ECO:0000313|Proteomes:UP000054502};
RA   McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JUL-2014) 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:KGF05582.1}.
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DR   EMBL; JRMX01000014; KGF05582.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A095YGA2; -.
DR   STRING; 1219585.HMPREF1631_04685; -.
DR   eggNOG; COG0294; Bacteria.
DR   OrthoDB; 9811744at2; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000054502; 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.
DR   InterPro; IPR006390; DHP_synth_dom.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
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:UP000054502};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361205}.
FT   DOMAIN          1..255
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   267 AA;  28478 MW;  34F6BDD0F025DB3C CRC64;
     MKIMGIVNVT PDSFSDGGMW DTPEKAVAHG RSLLCLGADV LDIGGESTRP GARSLDSATE
     WDRIAPVVTD LAREGCVSVD TYHARTAELA VRAGAKIVND VTGGKGDPEM FAAVADLGCE
     YILQHGRGNA RTMNSLSNYE SGVAQTVLAE LLRARDRAVA AGIDAQKIIL DPGLGFAKLG
     DQDWELLRHT EMFVNTGHRV LIGQSRKRFL QAVCGAESSF PQRDTATAVI SAFLSGMGVW
     AVRVHNVQAS AQAVATAEKL GKTRETR
//
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