PHP_MYCTU
ID PHP_MYCTU Reviewed; 326 AA.
AC P9WHN9; L0T4R7; P96413;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Phosphotriesterase homology protein;
GN Name=php; OrderedLocusNames=Rv0230c; ORFNames=MTCY08D5.26c;
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 AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) IN COMPLEX WITH ZINC, AND
RP CARBOXYLATION AT LYS-145.
RA Zhang L., Li X., Rao Z.H.;
RT "Crystallization and structure of the phosphotriesterase from Mycobacterium
RT tuberculosis.";
RL Submitted (DEC-2012) to the PDB data bank.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00679};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00679};
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.
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DR EMBL; AL123456; CCP42958.1; -; Genomic_DNA.
DR PIR; D70962; D70962.
DR RefSeq; NP_214744.1; NC_000962.3.
DR RefSeq; WP_003900835.1; NZ_NVQJ01000001.1.
DR PDB; 4IF2; X-ray; 2.27 A; A=1-326.
DR PDBsum; 4IF2; -.
DR AlphaFoldDB; P9WHN9; -.
DR SMR; P9WHN9; -.
DR STRING; 83332.Rv0230c; -.
DR PaxDb; P9WHN9; -.
DR DNASU; 886705; -.
DR GeneID; 886705; -.
DR KEGG; mtu:Rv0230c; -.
DR TubercuList; Rv0230c; -.
DR eggNOG; COG1735; Bacteria.
DR OMA; MVKCGFI; -.
DR PhylomeDB; P9WHN9; -.
DR BRENDA; 3.1.8.1; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009056; P:catabolic process; IEA:InterPro.
DR CDD; cd00530; PTE; 1.
DR InterPro; IPR017947; AryldialkylPase_Zn-BS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001559; Phosphotriesterase.
DR PANTHER; PTHR10819; PTHR10819; 1.
DR Pfam; PF02126; PTE; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS01322; PHOSPHOTRIESTERASE_1; 1.
DR PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..326
FT /note="Phosphotriesterase homology protein"
FT /id="PRO_0000205363"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00679,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:4IF2"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00679,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:4IF2"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00679,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:4IF2"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00679,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:4IF2"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00679,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:4IF2"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00679,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:4IF2"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00679,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:4IF2"
FT MOD_RES 145
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00679,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:4IF2"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:4IF2"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:4IF2"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:4IF2"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 43..59
FT /evidence="ECO:0007829|PDB:4IF2"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:4IF2"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:4IF2"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:4IF2"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4IF2"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:4IF2"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:4IF2"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:4IF2"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 155..171
FT /evidence="ECO:0007829|PDB:4IF2"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:4IF2"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:4IF2"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:4IF2"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:4IF2"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:4IF2"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:4IF2"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:4IF2"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 293..299
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 304..311
FT /evidence="ECO:0007829|PDB:4IF2"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:4IF2"
SQ SEQUENCE 326 AA; 35886 MW; C497D747B468005D CRC64;
MPELNTARGP IDTADLGVTL MHEHVFIMTT EIAQNYPEAW GDEDKRVAGA IARLGELKAR
GVDTIVDLTV IGLGRYIPRI ARVAAATELN IVVATGLYTY NDVPFYFHYL GPGAQLDGPE
IMTDMFVRDI EHGIADTGIK AGILKCATDE PGLTPGVERV LRAVAQAHKR TGAPISTHTH
AGLRRGLDQQ RIFAEEGVDL SRVVIGHCGD STDVGYLEEL IAAGSYLGMD RFGVDVISPF
QDRVNIVARM CERGHADKMV LSHDACCYFD ALPEELVPVA MPNWHYLHIH NDVIPALKQH
GVTDEQLHTM LVDNPRRIFE RQGGYQ
