ID   MPHES_MICSP             Reviewed;          20 AA.
AC   P84812;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Monoalkyl phthalate esterase;
DE            EC=3.1.1.-;
DE   Flags: Fragment;
OS   Micrococcus sp.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus;
OC   unclassified Micrococcus.
OX   NCBI_TaxID=1271;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=YGJ1 {ECO:0000269|PubMed:15713880};
RX   PubMed=15713880; DOI=10.1093/jb/mvi004;
RA   Maruyama K., Akita K., Naitou C., Yoshida M., Kitamura T.;
RT   "Purification and characterization of an esterase hydrolyzing monoalkyl
RT   phthalates from Micrococcus sp. YGJ1.";
RL   J. Biochem. 137:27-32(2005).
CC   -!- FUNCTION: Probably involved in the metabolism of xenobiotics and of
CC       natural substrates. Hydrolyzes medium-chain monoalkyl phthalate esters.
CC       {ECO:0000269|PubMed:15713880}.
CC   -!- ACTIVITY REGULATION: Inhibited by diethylpyrocarbonate, p-
CC       chloromercuribenzoate, Hg(2+) and Cu(2+). Not inhibited by the
CC       chelating reagents EDTA, 2,2'-dipyridyl, 1,10-phenanthroline, 8-
CC       hydroxyquinoline and tiron. {ECO:0000269|PubMed:15713880}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=280 nm {ECO:0000269|PubMed:15713880};
CC         Note=Exhibits a smaller absorbance peak at 290 nm and a minimum at
CC         250 nm. No significant absorption in the visible spectrum.
CC         {ECO:0000269|PubMed:15713880};
CC       pH dependence:
CC         Optimum pH is 7.5 with monobutyl phthalate as substrate. Retains 50%
CC         of maximum activity between pH 6.5 and pH 7.8.
CC         {ECO:0000269|PubMed:15713880};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius with monobutyl phthalate as
CC         substrate. {ECO:0000269|PubMed:15713880};
CC   -!- PTM: Exists in two forms, E1 and E2. E2 is probably produced by
CC       modification of E1. {ECO:0000269|PubMed:15713880}.
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DR   AlphaFoldDB; P84812; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042178; P:xenobiotic catabolic process; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   CHAIN           1..>20
FT                   /note="Monoalkyl phthalate esterase"
FT                   /id="PRO_0000232419"
FT   NON_TER         20
FT                   /evidence="ECO:0000303|PubMed:15713880"
SQ   SEQUENCE   20 AA;  2341 MW;  1A8B84A50702936E CRC64;
     SATAAREEYQ RKRSQFIEIG