ID A0A386HUW6_9BACT Unreviewed; 276 AA.
AC A0A386HUW6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
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:AYD49214.1};
GN ORFNames=D6B99_17235 {ECO:0000313|EMBL:AYD49214.1};
OS Arachidicoccus soli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Arachidicoccus.
OX NCBI_TaxID=2341117 {ECO:0000313|EMBL:AYD49214.1, ECO:0000313|Proteomes:UP000266118};
RN [1] {ECO:0000313|EMBL:AYD49214.1, ECO:0000313|Proteomes:UP000266118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIS59-12 {ECO:0000313|EMBL:AYD49214.1,
RC ECO:0000313|Proteomes:UP000266118};
RA Weon H.-Y., Kwon S.-W., Lee S.A.;
RT "Arachidicoccus sp. nov., a bacterium isolated from soil.";
RL Submitted (SEP-2018) 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}.
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DR EMBL; CP032489; AYD49214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A386HUW6; -.
DR KEGG; ark:D6B99_17235; -.
DR OrthoDB; 9811744at2; -.
DR Proteomes; UP000266118; 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 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:UP000266118};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AYD49214.1}.
FT DOMAIN 16..268
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 276 AA; 30023 MW; 7C9C30D7C1E6D241 CRC64;
MFTLNCKGKL LSLEKPAVMG IINVNNDSFY SGNRKAAIID AGALATKMLE EGAAILDLGG
QSTRPQSTLV SAKEEAERVI PVIESIIEKF PEVIVSIDTF YAEVAKEAVN AGASIVNDIS
AGNLDSKMLK TIAALDVPYI AMHMRGTPQT MNALTVYENI TREVLDYFIK KIEQCSSAGI
KDIIVDPGFG FAKTSVQSFE LMKNLNAFSM LERPILTGIS RKSMIYKTLN TTAEDALNGS
TVLHTFAVQN GANIIRTHDV KETVETIRLL EKLSVV
//
