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
//