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Database: UniProt
Entry: M0M6V7_9EURY
LinkDB: M0M6V7_9EURY
Original site: M0M6V7_9EURY 
ID   M0M6V7_9EURY            Unreviewed;       277 AA.
AC   M0M6V7;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE            EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN   ORFNames=C447_01695 {ECO:0000313|EMBL:EMA41527.1};
OS   Halococcus hamelinensis 100A6.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=1132509 {ECO:0000313|EMBL:EMA41527.1, ECO:0000313|Proteomes:UP000011566};
RN   [1] {ECO:0000313|EMBL:EMA41527.1, ECO:0000313|Proteomes:UP000011566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=100A6 {ECO:0000313|EMBL:EMA41527.1,
RC   ECO:0000313|Proteomes:UP000011566};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:EMA41527.1}.
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DR   EMBL; AOMB01000005; EMA41527.1; -; Genomic_DNA.
DR   RefSeq; WP_007690227.1; NZ_AOMB01000005.1.
DR   AlphaFoldDB; M0M6V7; -.
DR   PATRIC; fig|1132509.6.peg.400; -.
DR   eggNOG; arCOG02817; Archaea.
DR   OrthoDB; 371861at2157; -.
DR   Proteomes; UP000011566; 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   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; 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:UP000011566};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          17..260
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   277 AA;  29781 MW;  CAF0C58C81D64BCA CRC64;
     MQTVEAAGLP IGDDHPPRVM GVLNVSDEST YDPSVFTDPD EAASYVDGLV EEGADIVDIG
     LESANKRFEV LSADEELDRL DTALETLDRT ARDAVFSIET RYHEVAAAAL DAGFDMVNDI
     CGFADPEMAP TCEARDAAVV KMASPPDLTR PGALTSVDEI HDALARDLTD ETIVDPAFGG
     WSEAKTLDDD REIFHRLGEF RDLARPMLVS INRKNFLGEV VGRETDERLP ASLAATALAV
     ERGANVIRTH DVAETRDAAL IGDALGASDL ADPTAQR
//
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