ID K0VWS8_MYCFO Unreviewed; 261 AA.
AC K0VWS8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN ORFNames=MFORT_02463 {ECO:0000313|EMBL:EJZ15884.1};
OS Mycolicibacterium fortuitum subsp. fortuitum DSM 46621 = ATCC 6841 = JCM
OS 6387.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1214102 {ECO:0000313|EMBL:EJZ15884.1, ECO:0000313|Proteomes:UP000006043};
RN [1] {ECO:0000313|EMBL:EJZ15884.1, ECO:0000313|Proteomes:UP000006043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM46621 {ECO:0000313|Proteomes:UP000006043};
RX PubMed=23105073; DOI=10.1128/JB.01461-12;
RA Ho Y.S., Adroub S.A., Aleisa F., Mahmood H., Othoum G., Rashid F.,
RA Zaher M., Ali S., Bitter W., Pain A., Abdallah A.M.;
RT "Complete Genome Sequence of Mycobacterium fortuitum subsp. fortuitum Type
RT Strain DSM46621.";
RL J. Bacteriol. 194:6337-6338(2012).
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:EJZ15884.1}.
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DR EMBL; ALQB01000005; EJZ15884.1; -; Genomic_DNA.
DR AlphaFoldDB; K0VWS8; -.
DR PATRIC; fig|1214102.3.peg.492; -.
DR HOGENOM; CLU_008023_0_2_11; -.
DR Proteomes; UP000006043; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..254
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 261 AA; 27388 MW; 20EE4C85C7205B77 CRC64;
MNARSCPTPM RVMGVLNATP DSFWVDSRFD VTALAVAAGR RMFEAGAWAV DVGGESTRPG
AVPISVDEEL ARVLPVVAGL SDLGTVSVDT RNREVAEAAV RAGAGIINDV SGKLYDLAGR
LGVGYVSMHS HTVPVLAGVF PDYGDVVDEV TSFVTDVAQT ASAAGADPVW IDPGIGFGKS
TEHNLELLRR LPELCTCGFP VLLGVSRKTV IGHVTSREVV DRLAGSLAVI APAWAAGVDV
IRVHDVVETL DTITMLQAIW G
//
