ID   Y497_MYCPN              Reviewed;         351 AA.
AC   P75290;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2015, sequence version 4.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Uncharacterized protein MPN_497;
GN   OrderedLocusNames=MPN_497; ORFNames=MP346, P02_orf143;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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=AAB95994.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAB95994.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAB95994.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U00089; AAB95994.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S73672; S73672.
DR   RefSeq; NP_110185.1; NC_000912.1.
DR   AlphaFoldDB; P75290; -.
DR   SMR; P75290; -.
DR   IntAct; P75290; 3.
DR   STRING; 272634.MPN_497; -.
DR   EnsemblBacteria; AAB95994; AAB95994; MPN_497.
DR   KEGG; mpn:MPN_497; -.
DR   PATRIC; fig|272634.6.peg.539; -.
DR   HOGENOM; CLU_1804069_0_0_14; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009056; P:catabolic process; IEA:InterPro.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR001559; Phosphotriesterase.
DR   PANTHER; PTHR10819; PTHR10819; 2.
DR   Pfam; PF02126; PTE; 1.
DR   PIRSF; PIRSF016839; PhP; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..351
FT                   /note="Uncharacterized protein MPN_497"
FT                   /id="PRO_0000205368"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00679"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00679"
FT   BINDING         151
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         151
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         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00679"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00679"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00679"
FT   MOD_RES         151
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00679"
SQ   SEQUENCE   351 AA;  39121 MW;  E72651DB2ECD69DD CRC64;
     MKRFVRTVLG DIDPKDLGIC DCHDHLIKNW GPEAKEHPDF VMLSNEAAIK ECLEFVHHGG
     RSIVTMDPPN VGRDVKRMVA IAEQLKGKLN IIMATGFHKA AFYDKGSSWL AQVPVNEIVP
     MLVAEIEEGM DLYNYSGPVV KRGKAKAGII KAGTGYAAID RLELKALEAV AITSITTGAP
     VLVHTQLGTM AYEAAQHLID FGVNPRKIQL SHLNKNPDEY YYAKIIRELG VTLCFDGPDR
     VKYYPDCLLA KHIKYLVDLG FVKHITLALD AGRVLYQKHY GLEKGKECFG FAYLFERFIP
     LLKEVGVSDA AINTILVENL AEILAFDAPR QFNPKAVHPR VLALKKQLKI E