ID   PHP_MYCTO               Reviewed;         326 AA.
AC   P9WHN8; L0T4R7; P96413;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Phosphotriesterase homology protein;
GN   Name=php; OrderedLocusNames=MT0240;
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   -!- 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   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK44461.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK44461.1; ALT_INIT; Genomic_DNA.
DR   PIR; D70962; D70962.
DR   RefSeq; WP_003900835.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHN8; -.
DR   SMR; P9WHN8; -.
DR   EnsemblBacteria; AAK44461; AAK44461; MT0240.
DR   KEGG; mtc:MT0240; -.
DR   PATRIC; fig|83331.31.peg.261; -.
DR   HOGENOM; CLU_054760_1_0_11; -.
DR   Proteomes; UP000001020; 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   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..326
FT                   /note="Phosphotriesterase homology protein"
FT                   /id="PRO_0000428152"
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   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00679"
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   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   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00679"
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   BINDING         264
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00679"
FT   MOD_RES         145
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00679"
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