GUB2_HORVU
ID GUB2_HORVU Reviewed; 312 AA.
AC P12257;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Lichenase-2;
DE EC=3.2.1.73;
DE AltName: Full=(1->3,1->4)-beta-glucanase isoenzyme EII;
DE AltName: Full=Endo-beta-1,3-1,4 glucanase II;
DE AltName: Full=Lichenase II;
DE Flags: Precursor; Fragment;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-291, AND PROTEIN SEQUENCE OF 292-312.
RC STRAIN=cv. Himalaya;
RX PubMed=16593676; DOI=10.1073/pnas.83.7.2081;
RA Fincher G.B., Lock P.A., Morgan M.M., Lingelbach K., Wettenhall R.E.H.,
RA Mercer J.F.B., Brandt A., Thomsen K.K.;
RT "Primary structure of the (1-3,1-4)-beta-D-glucan 4-glucohydrolase from
RT barley aleurone.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2081-2085(1986).
RN [2]
RP PROTEIN SEQUENCE OF 7-46.
RC STRAIN=cv. Clipper; TISSUE=Seed;
RA Woodward J.R., Morgan F.J., Fincher G.B.;
RT "Amino acid sequence homology in two 1,3;1,4-beta-glucan endohydrolases
RT from germinating barley (Hordeum vulgare).";
RL FEBS Lett. 138:198-200(1982).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=8146192; DOI=10.1073/pnas.91.7.2785;
RA Varghese J.N., Garrett T.P.J., Colman P.M., Chen L., Hoej P.B.,
RA Fincher G.B.;
RT "Three-dimensional structures of two plant beta-glucan endohydrolases with
RT distinct substrate specificities.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2785-2789(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9452466; DOI=10.1074/jbc.273.6.3438;
RA Mueller J.J., Thomsen K.K., Heinemann U.;
RT "Crystal structure of barley 1,3-1,4-beta-glucanase at 2.0-A resolution and
RT comparison with Bacillus 1,3-1,4-beta-glucanase.";
RL J. Biol. Chem. 273:3438-3446(1998).
CC -!- FUNCTION: Functions in plant cell wall hydrolysis during mobilization
CC of the endosperm in germinating grain or during the growth of
CC vegetative tissues.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-
CC glucans containing (1->3)- and (1->4)-bonds.; EC=3.2.1.73;
CC -!- PATHWAY: Glycan metabolism; beta-D-glucan degradation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR EMBL; M13237; AAA32962.1; -; mRNA.
DR PIR; A25455; A25455.
DR PDB; 1AQ0; X-ray; 2.00 A; A/B=7-312.
DR PDB; 1GHR; X-ray; 2.20 A; A=7-312.
DR PDBsum; 1AQ0; -.
DR PDBsum; 1GHR; -.
DR AlphaFoldDB; P12257; -.
DR SMR; P12257; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR BRENDA; 3.2.1.73; 2687.
DR UniPathway; UPA00350; -.
DR EvolutionaryTrace; P12257; -.
DR ExpressionAtlas; P12257; baseline and differential.
DR GO; GO:0042972; F:licheninase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR000490; Glyco_hydro_17.
DR InterPro; IPR044965; Glyco_hydro_17_plant.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR32227; PTHR32227; 1.
DR Pfam; PF00332; Glyco_hydro_17; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycoprotein; Glycosidase;
KW Hydrolase; Signal.
FT SIGNAL <1..6
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 7..312
FT /note="Lichenase-2"
FT /id="PRO_0000011897"
FT ACT_SITE 99
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 238
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT NON_TER 1
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1AQ0"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:1AQ0"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1AQ0"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:1AQ0"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1AQ0"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1AQ0"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:1AQ0"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:1AQ0"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1AQ0"
FT STRAND 89..99
FT /evidence="ECO:0007829|PDB:1AQ0"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:1AQ0"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:1AQ0"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:1AQ0"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1AQ0"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1AQ0"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1AQ0"
FT HELIX 151..167
FT /evidence="ECO:0007829|PDB:1AQ0"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1AQ0"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:1AQ0"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:1GHR"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:1AQ0"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:1AQ0"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1AQ0"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:1AQ0"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:1AQ0"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:1AQ0"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:1AQ0"
FT HELIX 251..264
FT /evidence="ECO:0007829|PDB:1AQ0"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:1AQ0"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:1AQ0"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:1AQ0"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:1AQ0"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1AQ0"
SQ SEQUENCE 312 AA; 32774 MW; 7D18C2A6DF522E17 CRC64;
PPSVESIGVC YGMSANNLPA ASTVVSMFKF NGIKSMRLYA PNQAALQAVG GTGINVVVGA
PNDVLSNLAA SPAAAASWVK SNIQAYPKVS FRYVCVGNEV AGGATRNLVP AMKNVHGALV
AAGLGHIKVT TSVSQAILGV FSPPSAGSFT GEAAAFMGPV VQFLARTNAP LMANIYPYLA
WAYNPSAMDM GYALFNASGT VVRDGAYGYQ NLFDTTVDAF YTAMGKHGGS SVKLVVSESG
WPSGGGTAAT PANARFYNQH LINHVGRGTP RHPGAIETYI FAMFNENQKD SGVEQNWGLF
YPNMQHVYPI NF
