ID   CABM1_MACCH             Reviewed;          17 AA.
AC   P84783;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Carbamoylase-1;
DE            EC=3.-.-.-;
DE   AltName: Full=Carbamoylase I;
DE   Flags: Fragment;
OS   Mactra chinensis (Chinese surf clam).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Heteroconchia; Euheterodonta; Imparidentia; Neoheterodontei;
OC   Venerida; Mactroidea; Mactridae; Mactra.
OX   NCBI_TaxID=339787;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Digestive gland {ECO:0000269|PubMed:15501292};
RX   PubMed=15501292; DOI=10.1016/j.toxicon.2004.07.024;
RA   Lin H.-P., Cho Y., Yashiro H., Yamada T., Oshima Y.;
RT   "Purification and characterization of paralytic shellfish toxin
RT   transforming enzyme from Mactra chinensis.";
RL   Toxicon 44:657-668(2004).
CC   -!- FUNCTION: Hydrolysis of carbamoyl and sulfocarbamoyl esters of
CC       paralytic shellfish toxins. Ester hydrolysis is unaffected by the
CC       presence or absence of a hydroxyl moiety at the N-1 postion of the
CC       substrate toxin but is significantly affected by the stereochemistry of
CC       sulfate esters at C-11 of the substrate toxin.
CC       {ECO:0000269|PubMed:15501292}.
CC   -!- ACTIVITY REGULATION: Strongly inhibited by the serine proteinase
CC       inhibitors BSF and AEBSF. Weakly inhibited by the proteinase inhibitors
CC       bestatin and E-64, and by the serine proteinase inhibitor leupeptin.
CC       Not inhibited by EDTA or by the proteinase inhibitor aprotinin.
CC       {ECO:0000269|PubMed:15501292}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.02 uM for saxitoxin {ECO:0000269|PubMed:15501292};
CC         Vmax=40.1 pmol/min/ug enzyme {ECO:0000269|PubMed:15501292};
CC       pH dependence:
CC         Optimum pH is 7.0. Activity decreases sharply with increasing acidity
CC         or alkalinity. {ECO:0000269|PubMed:15501292};
CC       Temperature dependence:
CC         Optimum temperature is 20 degrees Celsius and activity decreases
CC         sharply above 40 degrees Celsius. {ECO:0000269|PubMed:15501292};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15501292}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous (at protein level). Highest levels of
CC       expression in digestive gland and crystalline style.
CC       {ECO:0000269|PubMed:15501292}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:15501292}.
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DR   PRIDE; P84783; -.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:UniProtKB.
DR   GO; GO:0009403; P:toxin biosynthetic process; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Hydrolase.
FT   CHAIN           1..>17
FT                   /note="Carbamoylase-1"
FT                   /id="PRO_0000227530"
FT   UNSURE          12
FT                   /note="D or G"
FT                   /evidence="ECO:0000269|PubMed:15501292"
FT   UNSURE          14
FT                   /note="I or V"
FT                   /evidence="ECO:0000269|PubMed:15501292"
FT   NON_TER         17
FT                   /evidence="ECO:0000303|PubMed:15501292"
SQ   SEQUENCE   17 AA;  1973 MW;  EE5AD4FE1281E280 CRC64;
     VRTPVTVQTK VDNIKXY