ID   CANHY_HELVI             Reviewed;          43 AA.
AC   P86355;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   02-JUN-2021, entry version 11.
DE   RecName: Full=Canavanine hydrolase {ECO:0000303|PubMed:9122181};
DE            Short=CH {ECO:0000303|PubMed:9122181};
DE            EC=3.-.-.-;
DE   Flags: Fragments;
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   TISSUE=Larval gut {ECO:0000269|PubMed:9122181};
RX   PubMed=9122181; DOI=10.1073/pnas.94.6.2255;
RA   Melangeli C., Rosenthal G.A., Dalman D.L.;
RT   "The biochemical basis for L-canavanine tolerance by the tobacco budworm
RT   Heliothis virescens (Noctuidae).";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:2255-2260(1997).
CC   -!- FUNCTION: Irreversibly hydrolyzes L-canavanine to L-homoserine and
CC       hydroxyguanidine. Has no activity on L-2-amino-5-
CC       (guanidinooxy)pentanoate or L-2-amino-3-(guanidinooxy)propionate, or on
CC       the L-canavanine derivatives methyl-L-canavanine, L-canaline or O-
CC       ureido-L-homoserine. {ECO:0000269|PubMed:9122181}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.1 mM for L-canavanine {ECO:0000269|PubMed:9122181};
CC   -!- SUBUNIT: Hexamer, composed of two different subunits.
CC       {ECO:0000269|PubMed:9122181}.
CC   -!- CAUTION: The order of the peptides shown is unknown.
CC       {ECO:0000269|PubMed:9122181}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   CHAIN           <1..>43
FT                   /note="Canavanine hydrolase"
FT                   /id="PRO_0000392509"
FT   NON_CONS        15..16
FT                   /evidence="ECO:0000303|PubMed:9122181"
FT   NON_CONS        28..29
FT                   /evidence="ECO:0000303|PubMed:9122181"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:9122181"
FT   NON_TER         43
FT                   /evidence="ECO:0000303|PubMed:9122181"
SQ   SEQUENCE   43 AA;  4949 MW;  7C2B6F9DEBD8A6D5 CRC64;
     KFVPISCPMP TNRQPKSLVV NINENSVKKM PWFTNXXTYF GXT