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 27-MAR-2024, entry version 48.
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; Actinomycetota; Actinomycetes; Mycobacteriales; 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 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; 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:SF8; INACTIVE DIHYDROPTEROATE SYNTHASE 2; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 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..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
//
