ID I4EYP1_9ACTN Unreviewed; 211 AA.
AC I4EYP1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Dihydropteroate synthase 1 {ECO:0000313|EMBL:CCH88504.1};
DE EC=2.5.1.15 {ECO:0000313|EMBL:CCH88504.1};
GN OrderedLocusNames=MODMU_3079 {ECO:0000313|EMBL:CCH88504.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH88504.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH88504.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH88504.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
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DR EMBL; FO203431; CCH88504.1; -; Genomic_DNA.
DR AlphaFoldDB; I4EYP1; -.
DR STRING; 477641.MODMU_3079; -.
DR KEGG; mmar:MODMU_3079; -.
DR PATRIC; fig|477641.3.peg.2929; -.
DR eggNOG; COG0294; Bacteria.
DR HOGENOM; CLU_1303738_0_0_11; -.
DR Proteomes; UP000006461; 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-like.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
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 Reference proteome {ECO:0000313|Proteomes:UP000006461};
KW Transferase {ECO:0000313|EMBL:CCH88504.1}.
FT DOMAIN 1..152
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT REGION 160..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 211 AA; 22012 MW; B2FCCFC540B07ABD CRC64;
MAAGAVLVND VSPGSADART AAAWSPTRER AQYRDVAGEV ITGLEHRVAD AASSGTDPAQ
LIPDPGLGFA RQASHNWALL AGLDRLAPLR PPVLMGASRR TFLGQLLAAT DGRVHPAEQR
DAATLATTVL AAHTGAWGVR VHDVVPSIDA ARTVAAMGDE RSAVHGKAPT TAGQRALTRP
QDRSVITTAL SERLTSSSGH RRQASRDDVP T
//