ID A0A074MW92_9SPHN Unreviewed; 375 AA.
AC A0A074MW92;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN ORFNames=EH32_00160 {ECO:0000313|EMBL:KEO99276.1};
OS Erythrobacter litoralis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=39960 {ECO:0000313|EMBL:KEO99276.1, ECO:0000313|Proteomes:UP000027866};
RN [1] {ECO:0000313|EMBL:KEO99276.1, ECO:0000313|Proteomes:UP000027866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8509 {ECO:0000313|EMBL:KEO99276.1,
RC ECO:0000313|Proteomes:UP000027866};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. Strains.";
RL Submitted (APR-2014) 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:KEO99276.1}.
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DR EMBL; JMIX01000001; KEO99276.1; -; Genomic_DNA.
DR RefSeq; WP_034900495.1; NZ_JMIX01000001.1.
DR AlphaFoldDB; A0A074MW92; -.
DR KEGG; elq:Ga0102493_1160; -.
DR PATRIC; fig|39960.10.peg.2310; -.
DR OrthoDB; 9811744at2; -.
DR Proteomes; UP000027866; Unassembled WGS sequence.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:InterPro.
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; PS00792; DHPS_1; 1.
DR PROSITE; PS00793; DHPS_2; 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:UP000027866};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 101..355
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 375 AA; 39739 MW; D85EA313EEBDCAA3 CRC64;
MADVYLYPIT LASGPQAEAG EHGPGAIRLG GSMAYASRFA LVLREDGRVI DRRVFSVAEA
ERALDGLGPL EEVEARRQWA NLARVHAPIR ADERVIRLDQ PQVMGVLNVT PDSFSDGGAY
HDKEDEGRAH AAAMLEAGAA IIDIGGESTR PGAEATFETE EIERVVPAVR YCAAMGAAIS
VDSRRAGVIE QALAAGAHIA NDVSALRYDP RSSEVIESYG CPVVLMHAPG TGEDLHSGGG
YEDVVSEVFD FLRLARDKAI AGGIAEGNIV LDPGIGFGKS LADNLALLNA FPLFHALGSP
ILVGVSRKRM IGALSNEEGP KDRLAGSIAL AVRAMEAGVH ILRVHDVAET VQARNVWRGL
RDAALTDFSQ LPPLS
//
