ID Q08884_VICNA Unreviewed; 291 AA.
AC Q08884;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 2.
DT 22-FEB-2023, entry version 98.
DE SubName: Full=Narbonin {ECO:0000313|EMBL:CAA80979.1};
OS Vicia narbonensis (Narbonne vetch).
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; Hologalegina; IRL clade; Fabeae; Vicia.
OX NCBI_TaxID=3912 {ECO:0000313|EMBL:CAA80979.1};
RN [1] {ECO:0000313|EMBL:CAA80979.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cotyledon {ECO:0000313|EMBL:CAA80979.1};
RA Schlesier B., Manteuffel R., Rudolph A., Behlke J.;
RT "Studies on seed globulins from legumes. VII. Narbonin, a 2S globulin from
RT Vicia narbonensis L.";
RL Biochem. Physiol. Pflanz. 173:420-428(1978).
RN [2] {ECO:0000313|EMBL:CAA80979.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cotyledon {ECO:0000313|EMBL:CAA80979.1};
RA Nong V.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAA80979.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cotyledon {ECO:0000313|EMBL:CAA80979.1};
RA Hennig M., Pfeffer-Hennig S., Dauter Z., Wilson K.S., Schlesier B.,
RA Nong V.H.;
RT "Crystal-structure of narbonin at 1.8 A resolution.";
RL Acta Crystallogr. 51:177-189(1995).
RN [4] {ECO:0007829|PDB:1NAR}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-289.
RX PubMed=15299319; DOI=10.1107/S0907444994009807;
RA Hennig M., Pfeffer-Hennig S., Dauter Z., Wilson K.S., Schlesier B.,
RA Nong V.H.;
RT "Crystal structure of narbonin at 1.8 A resolution.";
RL Acta Crystallogr. D 51:177-189(1995).
RN [5] {ECO:0000313|EMBL:CAA80979.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cotyledon {ECO:0000313|EMBL:CAA80979.1};
RX PubMed=7787188; DOI=10.1007/BF00042038;
RA Nong V.H., Schlesier B., Bassuener R., Repik A., Horstmann C., Muentz K.;
RT "Narbonin, a novel 2S protein from Vicia narbonensis L. seeds: cDNA, gene
RT structure and developmentally regulated formation.";
RL Plant Mol. Biol. 28:61-72(1995).
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DR EMBL; Z25532; CAA80979.1; -; mRNA.
DR PIR; S56696; S56696.
DR PIR; S56698; S56698.
DR PIR; S71764; S71764.
DR PDB; 1NAR; X-ray; 1.80 A; A=2-291.
DR PDBsum; 1NAR; -.
DR AlphaFoldDB; Q08884; -.
DR SMR; Q08884; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR EvolutionaryTrace; Q08884; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06544; GH18_narbonin; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR000677; Chitinase-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR46476:SF13; 2, PUTATIVE, EXPRESSED-RELATED; 1.
DR PANTHER; PTHR46476; CHITINASE 2-LIKE; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR PRINTS; PR00551; 2SGLOBULIN.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1NAR}.
FT DOMAIN 4..291
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 291 AA; 33288 MW; DC8847C4DEC7307F CRC64;
MPKPIFREYI GVKPNSTTLH DFPTEIINTE TLEFHYILGF AIESYYESGK GTGTFEESWD
VELFGPEKVK NLKRRHPEVK VVISIGGRGV NTPFDPAEEN VWVSNAKESL KLIIQKYSDD
SGNLIDGIDI HYEHIRSDEP FATLMGQLIT ELKKDDDLNI NVVSIAPSEN NSSHYQKLYN
AKKDYINWVD YQFSNQQKPV STDDAFVEIF KSLEKDYHPH KVLPGFSTDP LDTKHNKITR
DIFIGGCTRL VQTFSLPGVF FWNANDSVIP KRDGDKPFIV ELTLQQLLAK R
//
