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CONB_CANEN
ID   CONB_CANEN              Reviewed;         324 AA.
AC   P49347;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Concanavalin B;
DE            Short=Con B;
DE   Flags: Precursor;
OS   Canavalia ensiformis (Jack bean) (Dolichos ensiformis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Canavalia.
OX   NCBI_TaxID=3823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Cotyledon;
RA   Schlesier B., Nong V., Horstmann C., Hennig M.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX   PubMed=7490746; DOI=10.1006/jmbi.1995.0614;
RA   Hennig M., Jansonius J.N., van Scheltinga A.C.T., Dijkstra B.W.,
RA   Schlesier B.;
RT   "Crystal structure of concanavalin B at 1.65-A resolution. An 'inactivated'
RT   chitinase from seeds of Canavalia ensiformis.";
RL   J. Mol. Biol. 254:237-246(1995).
CC   -!- FUNCTION: May act as a carbohydrate-binding protein.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR   EMBL; X83426; CAA58450.1; -; mRNA.
DR   PIR; S57649; S57649.
DR   PDB; 1CNV; X-ray; 1.65 A; A=26-324.
DR   PDB; 6CAF; X-ray; 1.30 A; A=1-324.
DR   PDB; 6GWA; X-ray; 2.10 A; A=26-324.
DR   PDBsum; 1CNV; -.
DR   PDBsum; 6CAF; -.
DR   PDBsum; 6GWA; -.
DR   AlphaFoldDB; P49347; -.
DR   SMR; P49347; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   EvolutionaryTrace; P49347; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR   InterPro; IPR045321; Cts1-like.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Glycoprotein; Signal.
FT   SIGNAL          1..25
FT   CHAIN           26..324
FT                   /note="Concanavalin B"
FT                   /id="PRO_0000011989"
FT   DOMAIN          30..311
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   STRAND          31..36
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   HELIX           39..41
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   HELIX           44..49
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   STRAND          54..61
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   TURN            76..78
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   HELIX           87..90
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   HELIX           91..99
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   STRAND          103..109
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   STRAND          111..115
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   HELIX           120..134
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   STRAND          135..139
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:6GWA"
FT   HELIX           164..178
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   STRAND          183..186
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   STRAND          189..193
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   TURN            195..197
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   HELIX           198..202
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   STRAND          207..212
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   TURN            217..219
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   HELIX           227..239
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   STRAND          240..242
FT                   /evidence="ECO:0007829|PDB:1CNV"
FT   STRAND          247..254
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   HELIX           255..257
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   HELIX           266..272
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   HELIX           274..276
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   HELIX           280..283
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   STRAND          284..290
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   HELIX           292..298
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   HELIX           300..308
FT                   /evidence="ECO:0007829|PDB:6CAF"
FT   TURN            309..312
FT                   /evidence="ECO:0007829|PDB:6CAF"
SQ   SEQUENCE   324 AA;  36728 MW;  539CA5D4B68397FE CRC64;
     MGCERKALIL MVVIWIMSFW TLSLADISST EIAVYWGQRE DGLLRDTCKT NNYKIVFISF
     LDKFGCEIRK PELELEGVCG PSVGNPCSFL ESQIKECQRM GVKVFLALGG PKGTYSACSA
     DYAKDLAEYL HTYFLSERRE GPLGKVALDG IHFDIQKPVD ELNWDNLLEE LYQIKDVYQS
     TFLLSAAPGC LSPDEYLDNA IQTRHFDYIF VRFYNDRSCQ YSTGNIQRIR NAWLSWTKSV
     YPRDKNLFLE LPASQATAPG GGYIPPSALI GQVLPYLPDL QTRYAGIALW NRQADKETGY
     STNIIRYLNA TAMPFTSNLL KYPS
 
 
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