ID H0J0F1_9GAMM Unreviewed; 271 AA.
AC H0J0F1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN ORFNames=MOY_05515 {ECO:0000313|EMBL:EHK61667.1};
OS Halomonas sp. GFAJ-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK61667.1, ECO:0000313|Proteomes:UP000004512};
RN [1] {ECO:0000313|EMBL:EHK61667.1, ECO:0000313|Proteomes:UP000004512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK61667.1,
RC ECO:0000313|Proteomes:UP000004512};
RX PubMed=22408239; DOI=10.1128/JB.06664-11;
RA Phung le T., Silver S., Trimble W.L., Gilbert J.A.;
RT "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256).";
RL J. Bacteriol. 194:1835-1836(2012).
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:EHK61667.1}.
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DR EMBL; AHBC01000021; EHK61667.1; -; Genomic_DNA.
DR AlphaFoldDB; H0J0F1; -.
DR STRING; 1118153.MOY_05515; -.
DR PATRIC; fig|1118153.6.peg.1112; -.
DR eggNOG; COG0294; Bacteria.
DR Proteomes; UP000004512; 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; 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:UP000004512};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..251
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 271 AA; 28848 MW; FA4A67EC7B18E394 CRC64;
MGILNVTPDS FSDGGQHVAL DDALRHAERM LAEGAVMIDV GGESTRPGAP AVSEQEELDR
VSPVVEALVR ELDALVSIDT SSPAVMRQAS ALGAGMINDV RALEREGALA AAIGSGLPVC
LMHRQGEPQN MQQSPRYEQP VESAVVAYLA ERVAACEAAG LRRNRLLLDP GFGFGKTVEH
NLRLLKYMDA LQALELPLLV GMSRKSMIGK VLGRPVEERL AGGLALTAMA VERGANIVRV
HDVGPTVDAV NMAWAVLQEG CEPPLNKEFD A
//
