SCBM1_MEGVE
ID SCBM1_MEGVE Reviewed; 94 AA.
AC P86101;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 15.
DE RecName: Full=Sulfocarbamoylase-1 {ECO:0000303|PubMed:18599388};
DE EC=3.1.1.-;
DE AltName: Full=Sulfocarbamoylase I {ECO:0000303|PubMed:18599388};
DE Flags: Fragments;
OS Megangulus venulosus (Japanese bivalve) (Tellina venulosa).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Heteroconchia; Euheterodonta; Imparidentia; Neoheterodontei;
OC Cardiida; Tellinoidea; Tellinidae; Megangulus.
OX NCBI_TaxID=2602932;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Crystalline style {ECO:0000269|PubMed:18599388};
RX PubMed=18599388; DOI=10.1016/j.bbapap.2008.05.008;
RA Cho Y., Ogawa N., Takahashi M., Lin H.-P., Oshima Y.;
RT "Purification and characterization of paralytic shellfish toxin-
RT transforming enzyme, sulfocarbamoylase I, from the Japanese bivalve
RT Peronidia venulosa.";
RL Biochim. Biophys. Acta 1784:1277-1285(2008).
CC -!- FUNCTION: Hydrolysis of sulfocarbamoyl esters of paralytic shellfish
CC toxins. Does not hydrolyze the carbamoyl esters of paralytic shellfish
CC toxins. Ester hydrolysis is significantly affected by the
CC stereochemistry of sulfate esters at C-11 of the substrate toxin.
CC {ECO:0000269|PubMed:18599388}.
CC -!- ACTIVITY REGULATION: Strongly inhibited by the serine proteinase
CC inhibitor AEBSF. Weakly inhibited by the proteinase inhibitors BSF and
CC aprotinin, and by EDTA. Not inhibited by the proteinase inhibitors
CC bestatin, E-64 and leupeptin. {ECO:0000269|PubMed:18599388}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. Activity decreases sharply with increasing acidity
CC or alkalinity. {ECO:0000269|PubMed:18599388};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius and activity decreases
CC sharply above 35 degrees Celsius. {ECO:0000269|PubMed:18599388};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18599388}.
CC -!- TISSUE SPECIFICITY: Ubiquitous (at protein level). Highest levels of
CC expression in crystalline style followed by digestive gland and mantle.
CC {ECO:0000269|PubMed:18599388}.
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DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:UniProtKB.
DR GO; GO:0009407; P:toxin catabolic process; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase.
FT CHAIN <1..>94
FT /note="Sulfocarbamoylase-1"
FT /id="PRO_0000355082"
FT UNSURE 2
FT /note="T or C"
FT /evidence="ECO:0000269|PubMed:18599388"
FT UNSURE 3
FT /note="E or C"
FT /evidence="ECO:0000269|PubMed:18599388"
FT UNSURE 12
FT /note="R or K"
FT /evidence="ECO:0000269|PubMed:18599388"
FT UNSURE 13
FT /note="T or C"
FT /evidence="ECO:0000269|PubMed:18599388"
FT UNSURE 14
FT /note="E or C"
FT /evidence="ECO:0000269|PubMed:18599388"
FT NON_CONS 11..12
FT /evidence="ECO:0000303|PubMed:18599388"
FT NON_CONS 22..23
FT /evidence="ECO:0000303|PubMed:18599388"
FT NON_CONS 33..34
FT /evidence="ECO:0000303|PubMed:18599388"
FT NON_CONS 44..45
FT /evidence="ECO:0000303|PubMed:18599388"
FT NON_CONS 53..54
FT /evidence="ECO:0000303|PubMed:18599388"
FT NON_CONS 64..65
FT /evidence="ECO:0000303|PubMed:18599388"
FT NON_CONS 73..74
FT /evidence="ECO:0000303|PubMed:18599388"
FT NON_CONS 85..86
FT /evidence="ECO:0000303|PubMed:18599388"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:18599388"
FT NON_TER 94
FT /evidence="ECO:0000303|PubMed:18599388"
SQ SEQUENCE 94 AA; 10291 MW; C400D3511C72E948 CRC64;
TTEEVPLNPE PRTECDSDNC AAGERPYAPN IAIENGDTII AIGVVADVMF VIDXNCPLYC
NFCIVADVMF VIDLVYEVGS FEALQQAIDN IMFT
