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Database: UniProt
Entry: E0UPT4_SULAO
LinkDB: E0UPT4_SULAO
Original site: E0UPT4_SULAO 
ID   E0UPT4_SULAO            Unreviewed;       379 AA.
AC   E0UPT4;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE            EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN   OrderedLocusNames=Saut_1699 {ECO:0000313|EMBL:ADN09743.1};
OS   Sulfurimonas autotrophica (strain ATCC BAA-671 / DSM 16294 / JCM 11897 /
OS   OK10).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=563040 {ECO:0000313|EMBL:ADN09743.1, ECO:0000313|Proteomes:UP000007803};
RN   [1] {ECO:0000313|EMBL:ADN09743.1, ECO:0000313|Proteomes:UP000007803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC   {ECO:0000313|Proteomes:UP000007803};
RX   PubMed=21304749;
RA   Sikorski J., Munk C., Lapidus A., Ngatchou Djao O.D., Lucas S.,
RA   Glavina Del Rio T., Nolan M., Tice H., Han C., Cheng J.F., Tapia R.,
RA   Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Sims D., Meincke L., Brettin T., Detter J.C.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Lang E., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Sulfurimonas autotrophica type strain
RT   (OK10).";
RL   Stand. Genomic Sci. 3:194-202(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC   {ECO:0000313|Proteomes:UP000007803};
RX   DOI=10.4056/sigs.1173118;
RA   Sikorski J., Munk C., Lapidus A., Djao O., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Sims D.,
RA   Meincke L., Brettin T., Detter J., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y., Jeffries C., Rohde M., Lang E., Spring S., Goker M.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA   Klenk H.;
RT   "Complete genome sequence of Sulfurimonas autotrophica type strain
RT   (OK10T).";
RL   Stand. Genomic Sci. 3:194-202(2010).
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; CP002205; ADN09743.1; -; Genomic_DNA.
DR   RefSeq; WP_013327496.1; NC_014506.1.
DR   AlphaFoldDB; E0UPT4; -.
DR   STRING; 563040.Saut_1699; -.
DR   KEGG; sua:Saut_1699; -.
DR   eggNOG; COG0294; Bacteria.
DR   HOGENOM; CLU_008023_1_0_7; -.
DR   OrthoDB; 9811744at2; -.
DR   Proteomes; UP000007803; 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; IPR016227; Dihydropteroate_synthase_prd.
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   PIRSF; PIRSF000501; DHPS_Campy_prd; 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:UP000007803};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADN09743.1}.
FT   DOMAIN          120..372
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   379 AA;  42044 MW;  1334195B3595B138 CRC64;
     MQVEKLSNDI NIKEQLKKLG VDEGGINILA SKATTHILYI HDLHVGAANI LKQDALSIGA
     DLAVPRGTVV AAKPRVDCIL IANTKQLRTL AKKELAQPFA LKELAKKLKE FIQIQKPESI
     DIMGIINAND DSFYARSRFK DRDAIQSIEQ MIEKGATIID IGAVSSRPNA PVVSVEEELA
     RIEPLLALIK KEKLYEKVKF SCDSYEPQVL QNALESGFTI INDITGLQND EVCRLCASYD
     AAAVIMHMQG NPQTMQKNPH YDNILSEVYD FFDERVQKAE SFGIKDIILD VGIGFGKTLE
     NNLVLLKNLE HFLTLQKPLL VGASRKSMIN KISPSDVEQR LAGTLALHLE ALKNGASILR
     VHDVFEHVQA LKVFRALSL
//
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