DHPS2_MYCTU
ID DHPS2_MYCTU Reviewed; 318 AA.
AC P9WNC9; 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 39.
DE RecName: Full=Inactive dihydropteroate synthase 2;
DE Short=DHPS 2;
DE AltName: Full=Dihydropteroate pyrophosphorylase 2;
GN Name=folP2; OrderedLocusNames=Rv1207; ORFNames=MTCI364.19;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 2-318, FUNCTION, SUBUNIT, AND
RP ABSENCE OF DIHYDROPTEROATE SYNTHASE ACTIVITY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18680522; DOI=10.1111/j.1574-6968.2008.01302.x;
RA Gengenbacher M., Xu T., Niyomrattanakit P., Spraggon G., Dick T.;
RT "Biochemical and structural characterization of the putative
RT dihydropteroate synthase ortholog Rv1207 of Mycobacterium tuberculosis.";
RL FEMS Microbiol. Lett. 287:128-135(2008).
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. {ECO:0000269|PubMed:18680522}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18680522}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP43963.1; -; Genomic_DNA.
DR PIR; E70609; E70609.
DR RefSeq; NP_215723.1; NC_000962.3.
DR RefSeq; WP_003406241.1; NZ_NVQJ01000039.1.
DR PDB; 2VP8; X-ray; 2.64 A; A/B=2-318.
DR PDBsum; 2VP8; -.
DR AlphaFoldDB; P9WNC9; -.
DR SMR; P9WNC9; -.
DR STRING; 83332.Rv1207; -.
DR PaxDb; P9WNC9; -.
DR DNASU; 887447; -.
DR GeneID; 45425177; -.
DR GeneID; 887447; -.
DR KEGG; mtu:Rv1207; -.
DR TubercuList; Rv1207; -.
DR eggNOG; COG0294; Bacteria.
DR OMA; DPGHDFG; -.
DR PhylomeDB; P9WNC9; -.
DR BRENDA; 2.5.1.15; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..318
FT /note="Inactive dihydropteroate synthase 2"
FT /id="PRO_0000168216"
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 STRAND 30..32
FT /evidence="ECO:0007829|PDB:2VP8"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2VP8"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2VP8"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2VP8"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:2VP8"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:2VP8"
FT HELIX 97..114
FT /evidence="ECO:0007829|PDB:2VP8"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:2VP8"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:2VP8"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:2VP8"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:2VP8"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:2VP8"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:2VP8"
FT HELIX 186..206
FT /evidence="ECO:0007829|PDB:2VP8"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2VP8"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:2VP8"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:2VP8"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:2VP8"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:2VP8"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2VP8"
FT HELIX 268..280
FT /evidence="ECO:0007829|PDB:2VP8"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:2VP8"
FT HELIX 291..304
FT /evidence="ECO:0007829|PDB:2VP8"
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
