EBM_ARATH
ID EBM_ARATH Reviewed; 944 AA.
AC Q75W54; O04029;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Mannosylglycoprotein endo-beta-mannosidase;
DE Short=AtEBM;
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; OrderedLocusNames=At1g09010; ORFNames=F7G19.12;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND MUTAGENESIS OF GLU-464 AND GLU-549.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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:15247239};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:15247239};
CC -!- SUBUNIT: Heterotrimer of 31 kDa, 28 kDa and 42 kDa subunits.
CC {ECO:0000250}.
CC -!- PTM: The mature enzyme is proteotically cleaved into 3 subunits of 31
CC kDa, 28 kDa and 42 kDa. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70407.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB122060; BAD15284.1; -; mRNA.
DR EMBL; AC000106; AAB70407.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28382.1; -; Genomic_DNA.
DR PIR; A86222; A86222.
DR RefSeq; NP_563833.2; NM_100772.5.
DR AlphaFoldDB; Q75W54; -.
DR SMR; Q75W54; -.
DR BioGRID; 22663; 1.
DR STRING; 3702.AT1G09010.1; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PaxDb; Q75W54; -.
DR PRIDE; Q75W54; -.
DR ProteomicsDB; 224714; -.
DR EnsemblPlants; AT1G09010.1; AT1G09010.1; AT1G09010.
DR GeneID; 837422; -.
DR Gramene; AT1G09010.1; AT1G09010.1; AT1G09010.
DR KEGG; ath:AT1G09010; -.
DR Araport; AT1G09010; -.
DR TAIR; locus:2036094; AT1G09010.
DR eggNOG; KOG2230; Eukaryota.
DR HOGENOM; CLU_005015_2_1_1; -.
DR InParanoid; Q75W54; -.
DR OMA; VDWNPYP; -.
DR OrthoDB; 517710at2759; -.
DR PhylomeDB; Q75W54; -.
DR BioCyc; ARA:AT1G09010-MON; -.
DR BRENDA; 3.2.1.152; 399.
DR PRO; PR:Q75W54; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q75W54; baseline and differential.
DR Genevisible; Q75W54; AT.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
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:SF4; PTHR43536:SF4; 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 Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..262
FT /note="Mannosylglycoprotein endo-beta-mannosidase 31 kDa
FT subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000045502"
FT CHAIN 263..491
FT /note="Mannosylglycoprotein endo-beta-mannosidase 28 kDa
FT subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000045503"
FT CHAIN 492..944
FT /note="Mannosylglycoprotein endo-beta-mannosidase 42 kDa
FT subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000045504"
FT ACT_SITE 464
FT /note="Proton donor"
FT ACT_SITE 549
FT /note="Nucleophile"
FT MUTAGEN 464
FT /note="E->A: Loss of activity in vitro."
FT /evidence="ECO:0000269|PubMed:15247239"
FT MUTAGEN 549
FT /note="E->A: Loss of activity in vitro."
FT /evidence="ECO:0000269|PubMed:15247239"
SQ SEQUENCE 944 AA; 107661 MW; EE2D77A2DC54E6F3 CRC64;
MAEIGKTVLD FGWIAARSTE VDVNGVQLTT TNPPAISSES RWMEAAVPGT VLGTLVKNKA
IPDPFYGLEN EAITDIADSG RDYYTFWFFT KFQCQRLLNQ YVHLNFRAIN YSAQVFVNGH
KTELPKGMFR RHTLDVTDIL HPESNLLALI VHPPDHPGTI PPEGGQGGDH EIGKDVAAQY
VQGWDWICPI RDRNTGIWDE VSISVTGPVR IIDPHLVSTF FDDYKRAYLH VTAELENKST
WNTECSVNIQ ITAELENGVC LVEHLQTENV LIPAQGRIQH TFKPLYFYKP ELWWPNGMGK
QNLYDILITV VVNEFGESDS WMQPFGFRKI ESVIDSVTGG RLFKINGEPI FIRGGNWILS
DGLLRLSKER YRTDIKFHAD MNMNMIRCWG GGLAERPEFY HFCDIYGLLV WQEFWITGDV
DGRGVPVSNP NGPLDHELFL LCARDTVKLL RNHPSLALWV GGNEQVPPKD INEALKQDLR
LHSYFETQLL SDKDSDPSVY LDGTRVYIQG SMWDGFADGK GNFTDGPYEI QYPEDFFKDT
YYKYGFNPEV GSVGMPVAET IRATMPPEGW TIPLFKKGLD GFIKEVPNRM WDYHKYIPYS
NPGKVHDQIL MYGTPENLDD FCLKAQLVNY IQYRALFEGW SSQMWTKYTG VLIWKNQNPW
TGLRGQFYDH LLDQTASFYG CRSAAEPVHV QLNLASYFVE VVNTTSKELS DVAIEASVWD
LDGNCPYYKV FKIVSAPPKK VVKISEFKYP KAANPKHVYF LLLKLYTVSD KAVISRNFYW
LHLPGKNYTL LEPYRKKQIP LKITCNAVMV GSRYELEVNV HNTSRANLAK NVVQEDEKRD
LGLLQKLFSR CVVSADSNRG LKVVEMKGSD SGVAFFLRFS VHNAETEKQD TRILPVHYSD
NYFSLVPGES MSFKISFAAP TGMKKSPRVM LQGWNYPDRF SVFG
