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Database: UniProt
Entry: D6ZBT2_SEGRD
LinkDB: D6ZBT2_SEGRD
Original site: D6ZBT2_SEGRD 
ID   D6ZBT2_SEGRD            Unreviewed;       285 AA.
AC   D6ZBT2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE            EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN   OrderedLocusNames=Srot_0422 {ECO:0000313|EMBL:ADG96909.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM
OS   44985 / JCM 13578).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96909.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96909.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M., Schneider S.,
RA   Bruce D., Goodwin L., Pitluck S., Liolios K., Mikhailova N., Pati A.,
RA   Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chertkov O., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Detter J.C., Han C.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(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; CP001958; ADG96909.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6ZBT2; -.
DR   STRING; 640132.Srot_0422; -.
DR   KEGG; srt:Srot_0422; -.
DR   eggNOG; COG0294; Bacteria.
DR   HOGENOM; CLU_008023_0_2_11; -.
DR   OMA; HMQGEPR; -.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR   InterPro; IPR045031; DHP_synth.
DR   InterPro; IPR006390; DHP_synth_dom.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
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:UP000002247};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADG96909.1}.
FT   DOMAIN          5..271
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   285 AA;  28764 MW;  E678E70AEDEB2D56 CRC64;
     MTPALTIMGV LNCTPDSFSG DGLASAPRGA GEAAVRAGLR LVAEGADIVD VGGESTRPGA
     AQVDPSEQLE RILPAVRGLA AAGVFVSVDT CAAAVARAAL AQGARMVNDV AGGLCDPELL
     TAAAEAGAWL VLGHWPGAPA RDHGYRPGGT TAALVAQELS ERAGAALAAG VARDRIILDP
     GLGFGKNTEE NWALIRGVHE LRATGFPVLI GASRKRFLGS GLPLASGHAE ADQAELVWRE
     AGTTAVTALA ATLGAWGVRV HAPRPNRAAA RAAAEFTGEG AHHHG
//
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