ID   DHPS2_MYCTO             Reviewed;         318 AA.
AC   P9WNC8; L0T8Y8; O05308; P64139;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Inactive dihydropteroate synthase 2;
DE            Short=DHPS 2;
DE   AltName: Full=Dihydropteroate pyrophosphorylase 2;
GN   Name=folP2; OrderedLocusNames=MT1245;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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}.
CC   -!- CAUTION: A histidine residue in the pterin-binding domain interferes
CC       with substrate binding, and seems to be responsible for abolishing
CC       dihydropteroate synthase activity. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45502.1; -; Genomic_DNA.
DR   PIR; E70609; E70609.
DR   RefSeq; WP_003406241.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNC8; -.
DR   SMR; P9WNC8; -.
DR   EnsemblBacteria; AAK45502; AAK45502; MT1245.
DR   GeneID; 45425177; -.
DR   KEGG; mtc:MT1245; -.
DR   PATRIC; fig|83331.31.peg.1346; -.
DR   HOGENOM; CLU_008023_0_0_11; -.
DR   Proteomes; UP000001020; 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;
FT   CHAIN           1..318
FT                   /note="Inactive dihydropteroate synthase 2"
FT                   /id="PRO_0000427149"
FT   DOMAIN          42..299
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            220
FT                   /note="Characteristic for family members without
FT                   dihydropteroate synthase activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   318 AA;  33046 MW;  918057B69AAA8E65 CRC64;
     MRSTPPASAG RSTPPALAGH STPPALAGHS TLCGRPVAGD RALIMAIVNR TPDSFYDKGA
     TFSDAAARDA VHRAVADGAD VIDVGGVKAG PGERVDVDTE ITRLVPFIEW LRGAYPDQLI
     SVDTWRAQVA KAACAAGADL INDTWGGVDP AMPEVAAEFG AGLVCAHTGG ALPRTRPFRV
     SYGTTTRGVV DAVISQVTAA AERAVAAGVA REKVLIDPAH DFGKNTFHGL LLLRHVADLV
     MTGWPVLMAL SNKDVVGETL GVDLTERLEG TLAATALAAA AGARMFRVHE VAATRRVLEM
     VASIQGVRPP TRTVRGLA