DHPS_STAAM
ID DHPS_STAAM Reviewed; 267 AA.
AC P64141; Q99W89;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Dihydropteroate synthase;
DE Short=DHPS;
DE EC=2.5.1.15;
DE AltName: Full=Dihydropteroate pyrophosphorylase;
GN Name=folP; OrderedLocusNames=SAV0514;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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:0000250|UniProtKB:P0AC13}.
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:0000250|UniProtKB:P0AC13};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0AC13};
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
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DR EMBL; BA000017; BAB56676.1; -; Genomic_DNA.
DR RefSeq; WP_000167944.1; NC_002758.2.
DR PDB; 4HB7; X-ray; 1.95 A; A/B=1-267.
DR PDBsum; 4HB7; -.
DR AlphaFoldDB; P64141; -.
DR SMR; P64141; -.
DR World-2DPAGE; 0002:P64141; -.
DR PaxDb; P64141; -.
DR EnsemblBacteria; BAB56676; BAB56676; SAV0514.
DR KEGG; sav:SAV0514; -.
DR HOGENOM; CLU_008023_0_2_9; -.
DR OMA; FSIDTYH; -.
DR PhylomeDB; P64141; -.
DR BioCyc; SAUR158878:SAV_RS02820-MON; -.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000002481; Chromosome.
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; -; 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 PANTHER; PTHR20941; PTHR20941; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR TIGRFAMs; TIGR01496; DHPS; 1.
DR PROSITE; PS00792; DHPS_1; 1.
DR PROSITE; PS00793; DHPS_2; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Folate biosynthesis; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..267
FT /note="Dihydropteroate synthase"
FT /id="PRO_0000168221"
FT DOMAIN 1..251
FT /note="Pterin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WND1"
FT BINDING 51
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 84
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 103
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 167
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 203
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 239..241
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:4HB7"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:4HB7"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:4HB7"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:4HB7"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:4HB7"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:4HB7"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:4HB7"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:4HB7"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:4HB7"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:4HB7"
FT HELIX 139..156
FT /evidence="ECO:0007829|PDB:4HB7"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:4HB7"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:4HB7"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:4HB7"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:4HB7"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:4HB7"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:4HB7"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4HB7"
FT HELIX 220..233
FT /evidence="ECO:0007829|PDB:4HB7"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:4HB7"
FT HELIX 243..262
FT /evidence="ECO:0007829|PDB:4HB7"
SQ SEQUENCE 267 AA; 29533 MW; A2E41F5C5544D86C CRC64;
MTKTKIMGIL NVTPDSFSDG GKFNNVETAI NRVKAMIDEG ADIIDVGGVS TRPGHEMVTL
EEELNRVLPV VEAIVGFDVK ISVDTFRSEV AEACLKLGVD MINDQWAGLY DHRMFQIVAK
YDAEIILMHN GNGNRDEPVV EEMLTSLLAQ AHQAKIAGIP SNKIWLDPGI GFAKTRNEEA
EVMARLDELV ATEYPVLLAT SRKRFTKEMM GYDTTPVERD EVTAATTAYG IMKGVRAVRV
HNVELNAKLA KGIDFLKENE NARHNLS
