ID A0A0U1KW05_9FIRM Unreviewed; 400 AA.
AC A0A0U1KW05;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Dihydropteroate synthase {ECO:0000256|ARBA:ARBA00016919};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
DE AltName: Full=Dihydropteroate pyrophosphorylase {ECO:0000256|ARBA:ARBA00030193};
GN ORFNames=SpAn4DRAFT_3970 {ECO:0000313|EMBL:CQR71465.1};
OS Sporomusa ovata.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=2378 {ECO:0000313|EMBL:CQR71465.1, ECO:0000313|Proteomes:UP000049855};
RN [1] {ECO:0000313|Proteomes:UP000049855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Nijsse Bart;
RL Submitted (MAR-2015) 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 -!- SIMILARITY: Belongs to the DHPS family.
CC {ECO:0000256|ARBA:ARBA00009503}.
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DR EMBL; CTRP01000004; CQR71465.1; -; Genomic_DNA.
DR RefSeq; WP_021167561.1; NZ_CTRP01000004.1.
DR AlphaFoldDB; A0A0U1KW05; -.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000049855; Unassembled WGS sequence.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC.
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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000049855};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CQR71465.1}.
FT DOMAIN 141..389
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 400 AA; 44025 MW; 442278B2F98E589A CRC64;
MQYNMRIIEI KNREQAQKEV AMVNCDPAGA AIMSNKAVYK TIKVENVVSK AALILKQTFL
SKGGEASVSR GAADYSSQYT DVLLSGSLKH FKQCIPQLKV QPWGLKKLAE ELEAIIAVDE
KFPQRSYKLG AHTLSVSPEK TLIMGILNIT PDSFSDGGKF NNIDVALKHV EQMIKEGADI
IDIGAESTRP YGSHKISAEE ELERLMPILE KVLDTFSIPI SIDTYKASVA RETLKAGAHI
INDIWGLQFD PEMAKVAAEY NVPVVIMYNQ GEAEYQRDIM SHMLEFLRRS MQIGETAGIR
PDNFIVDPGI GFVKKGSDNL VIMARLDELK SLGCPVLLGT SRKRFIGDIL DAPANDRVEG
TAATVALGIT KGANIVRVHD VKAIARVARM TDAMLNAKYK
//