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 27-MAR-2024, entry version 92. 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}. 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 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 Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR045321; Cts1-like. DR InterPro; IPR001223; Glyco_hydro18_cat. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR45708; ENDOCHITINASE; 1. DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1. DR Pfam; PF00704; Glyco_hydro_18; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 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 //