EBM_LILLO
ID EBM_LILLO Reviewed; 953 AA.
AC Q5H7P5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 4.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Mannosylglycoprotein endo-beta-mannosidase;
DE Short=Endo-beta-mannosidase;
DE EC=3.2.1.152;
DE Contains:
DE RecName: Full=Mannosylglycoprotein endo-beta-mannosidase 31 kDa subunit;
DE Contains:
DE RecName: Full=Mannosylglycoprotein endo-beta-mannosidase 28 kDa subunit;
DE Contains:
DE RecName: Full=Mannosylglycoprotein endo-beta-mannosidase 42 kDa subunit;
GN Name=EBM;
OS Lilium longiflorum (Trumpet lily).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Lilium.
OX NCBI_TaxID=4690;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND TISSUE SPECIFICITY.
RX PubMed=15713887; DOI=10.1093/jb/mvi008;
RA Sasaki A., Ishimizu T., Hase S.;
RT "Substrate specificity and molecular cloning of the lily endo-beta-
RT mannosidase acting on N-glycan.";
RL J. Biochem. 137:87-93(2005).
RN [2]
RP PROTEIN SEQUENCE OF 2-24; 60-69; 172-183; 347-361; 374-384; 497-521 AND
RP 876-887, SUBUNIT, AND CLEAVAGE.
RX PubMed=15247239; DOI=10.1074/jbc.m406886200;
RA Ishimizu T., Sasaki A., Okutani S., Maeda M., Yamagishi M., Hase S.;
RT "Endo-beta-mannosidase, a plant enzyme acting on N-glycan: purification,
RT molecular cloning, and characterization.";
RL J. Biol. Chem. 279:38555-38562(2004).
CC -!- FUNCTION: Glycosidase that specifically hydrolyzes the Man-beta-1,4-
CC GlcNAc linkage in the trimannosyl core structure of N-glycans. Does not
CC hydrolyzes pyridylamino derivatives sugar chains containing Man-alpha-
CC 1,3-Man-beta or Xylose-beta-1,2-Man-beta.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the alpha-D-mannosyl-(1->6)-beta-D-mannosyl-
CC (1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-
CC glucosaminyl sequence of glycoprotein to alpha-D-mannosyl-(1->6)-D-
CC mannose and N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-
CC glucosaminyl sequences.; EC=3.2.1.152;
CC Evidence={ECO:0000269|PubMed:15713887};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for Manalpha1-6Manbeta1-4GlcNAcbeta1-4GlcNAc-PA
CC {ECO:0000269|PubMed:15713887};
CC KM=75 uM for Manalpha1-6Manbeta1-4GlcNAcbeta1-4GlcNAc-peptide
CC {ECO:0000269|PubMed:15713887};
CC -!- SUBUNIT: Heterotrimer of 31 kDa, 28 kDa and 42 kDa subunits.
CC {ECO:0000269|PubMed:15247239}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:15713887}.
CC -!- PTM: The mature enzyme is proteotically cleaved into 3 subunits of 31
CC kDa, 28 kDa and 42 kDa. {ECO:0000269|PubMed:15247239}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR EMBL; AB185918; BAD89079.2; -; mRNA.
DR AlphaFoldDB; Q5H7P5; -.
DR SMR; Q5H7P5; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PRIDE; Q5H7P5; -.
DR BRENDA; 3.2.1.152; 3020.
DR SABIO-RK; Q5H7P5; -.
DR GO; GO:0033947; F:mannosylglycoprotein endo-beta-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR043534; EBDG/EBM.
DR InterPro; IPR028787; Endo-b-mannosidase.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041351; Ig_GlcNase.
DR PANTHER; PTHR43536; PTHR43536; 1.
DR PANTHER; PTHR43536:SF5; PTHR43536:SF5; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF18368; Ig_GlcNase; 1.
DR SUPFAM; SSF49303; SSF49303; 3.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycosidase; Hydrolase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15247239"
FT CHAIN 2..259
FT /note="Mannosylglycoprotein endo-beta-mannosidase 31 kDa
FT subunit"
FT /id="PRO_0000045505"
FT CHAIN 260..496
FT /note="Mannosylglycoprotein endo-beta-mannosidase 28 kDa
FT subunit"
FT /id="PRO_0000045506"
FT CHAIN 497..953
FT /note="Mannosylglycoprotein endo-beta-mannosidase 42 kDa
FT subunit"
FT /id="PRO_0000045507"
FT ACT_SITE 461
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 553
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 953 AA; 108181 MW; 744D9161460A1A6B CRC64;
MGKQVLDSGW LAARSTELEL TGVQLTTTRP PSGTSAPWIE AVVPGTVLGT LLKNKLVPDP
FYGLNNEGIL DIYDSGREYY TFWFFKSFEC KLSENQHVSL NFRAINYSAE VYLNGHKEIL
PKGMFRRHSI DITDILHPDG KNMLAVLVHP PDHPGQIPPE GGQGGDHEIG KDVATQYVEG
WDWMAPIRDR NTGIWDEVSL YTSGPVKIAD VHLVSSFFDM FRRAYLHSTV ELENKSSWRA
ECSLTILVTT ELDGDFNLIE YHQTHELSIP PESVIQYTLP PLFFYKPNLW WPNGMGKQSL
YNVEITIAVK GFGDSDSWNN KFGFRQIESA IDEATGGRLF KVNGQRVFIR GGNWILSDGL
LRLSKKRYMT DIKFHADMNF NMIRCWGGGL AERPEFYHYC DIYGLLVWQE FWITGDCDGR
GIPVSNPNGP LDHALFLHCA RDTIKLLRNH ASLALWVGGN EQIPPEDINS ALKNDLKLHP
FFKHNGVTVI GEDMLSETED PSQYLDGTRV YIQGSMWEGF ANGKGDFTDG PYEIQNPEDF
FKDDFYSYGF NPEVGSVGVP VAATIRATMP PEGWQIPLFK RLSDGFIEEV PNPIWEYHKY
ISYSKPGKVH DQIVLYGQPT NLDDFCEKAQ LVNYVQYRAL LEGWTSRMWT KYTGVLIWKT
QNPWTGLRGQ FYDHLHDQTA GFYGCRCAAE PVHVQLNLAT YFIEVVNTTH EELSDVAIEV
SVWDLDGTCP YYKVIENVLV SPKKVLPITE LKYQGSKNAK PVYFVLLKLF RPSNTTILSR
NFYWLRLPGT DFKLLEPYRA IEAPLKLTSE VNIVGSAYKI QMRVQNLSKN LNSESVNFLA
NDEKSDLSKK EGYISRICSG FKNSGTDSLR VVETKGTGSG VAFFLHFSVH AVKKDENEIE
DLRILPVHYS DNYFSLVPGE TTNISISFEV PHGVTPRVSL RGWNCSEEHY SVL
