DHPS2_MYCLE
ID DHPS2_MYCLE Reviewed; 291 AA.
AC P0C0X2; P46812;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Inactive dihydropteroate synthase 2;
DE Short=DHPS 2;
DE AltName: Full=Dihydropteroate pyrophosphorylase 2;
GN Name=folP2; OrderedLocusNames=ML1063;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Has very low affinity for the DHPS substrate 6-hydroxymethyl-
CC 7,8-dihydropterin-pyrophosphate, but can bind the inhibitor dapsone.
CC Seems to lack dihydropteroate synthase activity, and does probably not
CC function in folate metabolism (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
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DR EMBL; U15180; AAA62918.1; -; Genomic_DNA.
DR EMBL; AL583920; CAC31444.1; -; Genomic_DNA.
DR PIR; T45179; T45179.
DR RefSeq; NP_301781.1; NC_002677.1.
DR RefSeq; WP_010908105.1; NC_002677.1.
DR AlphaFoldDB; P0C0X2; -.
DR SMR; P0C0X2; -.
DR STRING; 272631.ML1063; -.
DR DrugBank; DB00250; Dapsone.
DR EnsemblBacteria; CAC31444; CAC31444; CAC31444.
DR KEGG; mle:ML1063; -.
DR PATRIC; fig|272631.5.peg.1909; -.
DR Leproma; ML1063; -.
DR eggNOG; COG0294; Bacteria.
DR HOGENOM; CLU_008023_0_0_11; -.
DR OMA; DPGHDFG; -.
DR BRENDA; 2.5.1.15; 3504.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:InterPro.
DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro.
DR CDD; cd00739; DHPS; 1.
DR Gene3D; 3.20.20.20; -; 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 PANTHER; PTHR20941; PTHR20941; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR TIGRFAMs; TIGR01496; DHPS; 1.
DR PROSITE; PS00792; DHPS_1; 1.
DR PROSITE; PS00793; DHPS_2; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 3: Inferred from homology;
KW Reference proteome.
FT CHAIN 1..291
FT /note="Inactive dihydropteroate synthase 2"
FT /id="PRO_0000168214"
FT DOMAIN 15..272
FT /note="Pterin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT SITE 193
FT /note="Characteristic for family members without
FT dihydropteroate synthase activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 291 AA; 30851 MW; 4243E35BB0E4C60F CRC64;
MQSMLCGRPV AADRQLIMAI VNRTPDSFYD RGATFSDEAA RAAAHRAVAE GADVIDVGGV
KAGPGQGVDV DTEIARLVPF IEWLRSAYTD LLISVDTWRA EVARLACTAG ADLINDSWGG
ADPAMHEVAA ELGAGLVCSH TGGALPRTRP FRVSYGTTTR GVVDDVIRQV TAAAERAVAA
GVTRDSVLVD PTHDFGKNTF HGLLLLRHVD ELVKTGWPVL MSLSNKDFVG ETLGVGLTER
LEGTLAATAL AAAAGVRMFR VHEVVATRRV LEMVASIQGT RPPTRTVRGL A