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Entry: A0A1T4SS95_9ACTN
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ID   A0A1T4SS95_9ACTN        Unreviewed;       305 AA.
AC   A0A1T4SS95;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=SAMN02745673_03885 {ECO:0000313|EMBL:SKA31109.1};
OS   Marinactinospora thermotolerans DSM 45154.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Marinactinospora.
OX   NCBI_TaxID=1122192 {ECO:0000313|EMBL:SKA31109.1, ECO:0000313|Proteomes:UP000190637};
RN   [1] {ECO:0000313|EMBL:SKA31109.1, ECO:0000313|Proteomes:UP000190637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45154 {ECO:0000313|EMBL:SKA31109.1,
RC   ECO:0000313|Proteomes:UP000190637};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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}.
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DR   EMBL; FUWS01000011; SKA31109.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4SS95; -.
DR   STRING; 1122192.SAMN02745673_03885; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000190637; 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:UP000190637};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361205}.
FT   DOMAIN          19..279
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   305 AA;  32682 MW;  62F0B2DC2B6F1146 CRC64;
     MAAMASMMKL PGLPDLGRCL VMGVVNVTPD SFSDGGDWFD HGRAIEHGLR LVDEGADIID
     VGGESTRPGA QRVSRDEELR RIGPVVRELV RQGVPVSIDT MRAEVAEHAV EAGAALVNDV
     SGGLADPAMA RLVAKSGVAY VVMHWRGHSH DMQNRAVYTD VVHEVHEELR QRMEAMIAEG
     VDPGQIVLDP GLGFSKRPDR GHNWALLAEM DRFHELGRPL LIAGSRKRFL GRLLADADGR
     DRPFTECDAA TAALSTLAAA NGAWCVRVHD VAPTADAVRV AAAWSSGGAA LDEGRADPVG
     GRSRR
//
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