PPTH_MYCTU
ID PPTH_MYCTU Reviewed; 324 AA.
AC I6YEE1;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=[Acyl-carrier-protein] phosphodiesterase PptH {ECO:0000305};
DE Short=ACP phosphodiesterase PptH {ECO:0000305};
DE EC=3.1.4.14 {ECO:0000269|PubMed:30705156};
DE AltName: Full=Ppt hydrolase {ECO:0000303|PubMed:30705156};
GN Name=pptH {ECO:0000303|PubMed:30705156};
GN OrderedLocusNames=Rv2795c {ECO:0000312|EMBL:CCP45594.1};
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 FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=30705156; DOI=10.1126/science.aau8959;
RA Ballinger E., Mosior J., Hartman T., Burns-Huang K., Gold B., Morris R.,
RA Goullieux L., Blanc I., Vaubourgeix J., Lagrange S., Fraisse L., Sans S.,
RA Couturier C., Bacque E., Rhee K., Scarry S.M., Aube J., Yang G.,
RA Ouerfelli O., Schnappinger D., Ioerger T.R., Engelhart C.A.,
RA McConnell J.A., McAulay K., Fay A., Roubert C., Sacchettini J., Nathan C.;
RT "Opposing reactions in coenzyme A metabolism sensitize Mycobacterium
RT tuberculosis to enzyme inhibition.";
RL Science 363:0-0(2019).
RN [4]
RP ERRATUM OF PUBMED:30705156.
RX PubMed=31221826; DOI=10.1126/science.aay3546;
RA Ballinger E., Mosior J., Hartman T., Burns-Huang K., Gold B., Morris R.,
RA Goullieux L., Blanc I., Vaubourgeix J., Lagrange S., Fraisse L., Sans S.,
RA Couturier C., Bacque E., Rhee K., Scarry S.M., Aube J., Yang G.,
RA Ouerfelli O., Schnappinger D., Ioerger T.R., Engelhart C.A.,
RA McConnell J.A., McAulay K., Fay A., Roubert C., Sacchettini J., Nathan C.;
RT "Opposing reactions in coenzyme A metabolism sensitize Mycobacterium
RT tuberculosis to enzyme inhibition.";
RL Science 364:0-0(2019).
RN [5] {ECO:0007744|PDB:6UNC}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-310 IN COMPLEX WITH IRON AND
RP MANGANESE, AND COFACTOR.
RX PubMed=31886928; DOI=10.1002/pro.3813;
RA Mosior J., Bourland R., Soma S., Nathan C., Sacchettini J.;
RT "Structural insights into phosphopantetheinyl hydrolase PptH from
RT Mycobacterium tuberculosis.";
RL Protein Sci. 29:744-757(2020).
CC -!- FUNCTION: Catalyzes the hydrolysis of the phosphopantetheine group from
CC substrate holo-carrier proteins. {ECO:0000269|PubMed:30705156}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + holo-[ACP] = (R)-4'-phosphopantetheine + apo-[ACP] +
CC H(+); Xref=Rhea:RHEA:20537, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9690,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:61723, ChEBI:CHEBI:64479; EC=3.1.4.14;
CC Evidence={ECO:0000269|PubMed:30705156};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:31886928};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:31886928};
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is highly and selectively
CC resistant to the amidino-urea compound 1-[(2,6-diethylphenyl)-3-N-
CC ethylcarbamimodoyl]urea (compound 8918). {ECO:0000269|PubMed:30705156}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45594.1; -; Genomic_DNA.
DR RefSeq; NP_217311.1; NC_000962.3.
DR RefSeq; WP_003414151.1; NZ_NVQJ01000020.1.
DR PDB; 6UNC; X-ray; 2.50 A; A/B/C/D=2-310.
DR PDBsum; 6UNC; -.
DR AlphaFoldDB; I6YEE1; -.
DR SMR; I6YEE1; -.
DR STRING; 83332.Rv2795c; -.
DR PaxDb; I6YEE1; -.
DR PRIDE; I6YEE1; -.
DR DNASU; 888492; -.
DR GeneID; 888492; -.
DR KEGG; mtu:Rv2795c; -.
DR PATRIC; fig|83332.111.peg.3108; -.
DR TubercuList; Rv2795c; -.
DR eggNOG; COG1409; Bacteria.
DR OMA; PEFAMWC; -.
DR PhylomeDB; I6YEE1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0008770; F:[acyl-carrier-protein] phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Iron; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..324
FT /note="[Acyl-carrier-protein] phosphodiesterase PptH"
FT /id="PRO_0000451443"
FT BINDING 22
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:31886928"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:31886928"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:31886928"
FT BINDING 51
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:31886928"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:31886928"
FT BINDING 205
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:31886928"
FT BINDING 246
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:31886928"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:31886928"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:6UNC"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:6UNC"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:6UNC"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:6UNC"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:6UNC"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:6UNC"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:6UNC"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:6UNC"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:6UNC"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:6UNC"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6UNC"
FT HELIX 176..192
FT /evidence="ECO:0007829|PDB:6UNC"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:6UNC"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:6UNC"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:6UNC"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6UNC"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:6UNC"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:6UNC"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:6UNC"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:6UNC"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:6UNC"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:6UNC"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:6UNC"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:6UNC"
SQ SEQUENCE 324 AA; 37601 MW; AA32D2FCACE0F02A CRC64;
MTWKGSGQET VGAEPTLWAI SDLHTGHLGN KPVAESLYPS SPDDWLIVAG DVAERTDEIR
WSLDLLRRRF AKVIWVPGNH ELWTTNRDPM QIFGRARYDY LVNMCDEMGV VTPEHPFPVW
TERGGPATIV PMFLLYDYSF LPEGANSKAE GVAIAKERNV VATDEFLLSP EPYPTRDAWC
HERVAATRAR LEQLDWMQPT VLVNHFPLLR QPCDALFYPE FSLWCGTTKT ADWHTRYNAV
CSVYGHLHIP RTTWYDGVRF EEVSVGYPRE WRRRKPYSWL RQVLPDPQYA PGYLNDFGGH
FVITPEMRTQ AAQFRERLRQ RQSR
