ID J8SRM9_9PORP Unreviewed; 299 AA.
AC J8SRM9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN Name=folP {ECO:0000313|EMBL:EJU15434.1};
GN ORFNames=HMPREF1323_1034 {ECO:0000313|EMBL:EJU15434.1};
OS Porphyromonas sp. oral taxon 279 str. F0450.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1125723 {ECO:0000313|EMBL:EJU15434.1, ECO:0000313|Proteomes:UP000004156};
RN [1] {ECO:0000313|EMBL:EJU15434.1, ECO:0000313|Proteomes:UP000004156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0450 {ECO:0000313|EMBL:EJU15434.1,
RC ECO:0000313|Proteomes:UP000004156};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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:EJU15434.1}.
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DR EMBL; ALKJ01000048; EJU15434.1; -; Genomic_DNA.
DR RefSeq; WP_009433796.1; NZ_ALKJ01000048.1.
DR AlphaFoldDB; J8SRM9; -.
DR PATRIC; fig|1125723.3.peg.1652; -.
DR Proteomes; UP000004156; 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 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; PS50972; PTERIN_BINDING; 1.
PE 4: Predicted;
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000004156};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJU15434.1}.
FT DOMAIN 22..276
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 299 AA; 33186 MW; 5C0992E4947A2062 CRC64;
MSLTPAQTTL TLSGKLLTLE RPIVMGIVNV TPDSFFAGSR IAGETALRTR FDELVSEGAA
IADLGAYSSR PGADEVSVTE EMERLRPALR ILRDEYPDLP VSVDTFRSEV ARMAVEEYGA
AIINDISGGA LDPEMYRTVA ALQVPYILMH MKGDPQTMQS LTDYSDVTLD VIDYFTERIG
KLLELGLHDI ILDPGFGFSK TTEQNYELLM HLDDLTHTFT QPILVGVSRK SMIYRPLGCT
PAEALGGTTF LHALALERGA QILRVHDVRA AAEAITLYEQ ARPYLHREEH LHYSFTRSH
//
