ENAS1_ARATH
ID ENAS1_ARATH Reviewed; 680 AA.
AC F4JZC2; Q9FLA9;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Cytosolic endo-beta-N-acetylglucosaminidase 1 {ECO:0000305};
DE Short=ENGase 1 {ECO:0000305};
DE EC=3.2.1.96 {ECO:0000269|PubMed:21597164, ECO:0000269|PubMed:21796445};
DE AltName: Full=Endo-beta-N-acetyglucosaminidase 85A {ECO:0000303|PubMed:21796445};
DE Short=AtENGase85A {ECO:0000303|PubMed:21796445};
GN Name=ENGASE1 {ECO:0000305};
GN Synonyms=ENGASE85A {ECO:0000303|PubMed:21796445};
GN OrderedLocusNames=At5g05460 {ECO:0000312|Araport:AT5G05460};
GN ORFNames=K18I23.27 {ECO:0000312|EMBL:BAB09989.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [2]
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21597164; DOI=10.1271/bbb.110148;
RA Kimura Y., Takeoka Y., Inoue M., Maeda M., Fujiyama K.;
RT "Double-knockout of putative endo-beta-N-acetylglucosaminidase (ENGase)
RT genes in Arabidopsis thaliana: loss of ENGase activity induced accumulation
RT of high-mannose type free N-glycans bearing N,N'-acetylchitobiosyl unit.";
RL Biosci. Biotechnol. Biochem. 75:1019-1021(2011).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21796445; DOI=10.1007/s11103-011-9808-7;
RA Fischl R.M., Stadlmann J., Grass J., Altmann F., Leonard R.;
RT "The two endo-beta-N-acetylglucosaminidase genes from Arabidopsis thaliana
RT encode cytoplasmic enzymes controlling free N-glycan levels.";
RL Plant Mol. Biol. 77:275-284(2011).
CC -!- FUNCTION: Endoglycosidase that releases N-glycans from glycoproteins by
CC cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose
CC core. Involved in the production of high-mannose type N-glycans during
CC plant development and fruit maturation. {ECO:0000269|PubMed:21597164,
CC ECO:0000269|PubMed:21796445}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-
CC mannose glycopeptides and glycoproteins containing the
CC -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue
CC remains attached to the protein, the rest of the oligosaccharide is
CC released intact.; EC=3.2.1.96; Evidence={ECO:0000269|PubMed:21597164,
CC ECO:0000269|PubMed:21796445};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for dabsyl-Asn-Man5 {ECO:0000269|PubMed:21796445};
CC pH dependence:
CC Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:21796445};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21796445}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutants engase85A and engase85B accumulate
CC very high level of free N-glycans carrying two GlcNAc at the reducing
CC end, but their counterparts with a single GlcNAc are completely absent.
CC {ECO:0000269|PubMed:21597164, ECO:0000269|PubMed:21796445}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 85 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09989.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB010692; BAB09989.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90876.1; -; Genomic_DNA.
DR RefSeq; NP_196165.3; NM_120628.5.
DR AlphaFoldDB; F4JZC2; -.
DR SMR; F4JZC2; -.
DR STRING; 3702.AT5G05460.1; -.
DR CAZy; GH85; Glycoside Hydrolase Family 85.
DR PaxDb; F4JZC2; -.
DR PRIDE; F4JZC2; -.
DR ProteomicsDB; 220369; -.
DR EnsemblPlants; AT5G05460.1; AT5G05460.1; AT5G05460.
DR GeneID; 830429; -.
DR Gramene; AT5G05460.1; AT5G05460.1; AT5G05460.
DR KEGG; ath:AT5G05460; -.
DR Araport; AT5G05460; -.
DR TAIR; locus:2153579; AT5G05460.
DR eggNOG; KOG2331; Eukaryota.
DR HOGENOM; CLU_015297_1_0_1; -.
DR InParanoid; F4JZC2; -.
DR OMA; WGVLQSY; -.
DR OrthoDB; 722800at2759; -.
DR PRO; PR:F4JZC2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JZC2; baseline and differential.
DR Genevisible; F4JZC2; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0033925; F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity; IDA:TAIR.
DR GO; GO:0006491; P:N-glycan processing; IDA:TAIR.
DR GO; GO:0006517; P:protein deglycosylation; IGI:TAIR.
DR InterPro; IPR032979; ENGase.
DR InterPro; IPR005201; Glyco_hydro_85.
DR PANTHER; PTHR13246; PTHR13246; 1.
DR Pfam; PF03644; Glyco_hydro_85; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..680
FT /note="Cytosolic endo-beta-N-acetylglucosaminidase 1"
FT /id="PRO_0000432756"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 76351 MW; 1CB0D5D9AE80480A CRC64;
MSVAPPAPSP PPFDPTKPST PISFPIKTLQ DLKSRSYFDS FHYPFNRSSV PLRRNIGALS
DRPRLLVCHD MKGGYVDDKW VQGCGNNAGY AIWDWYLMDV FVYFSHSLVT LPPPCWTNTA
HRHGVKVLGT FITEWDEGKA TCKELLATKE SAQMYAERLA ELAAALGFDG WLINIENVID
EVQIPNLMVF VSHLTKVMHS SVPGGLVIWY DSVTIDGHLA WQDQLTENNK PFFDICDGIF
MNYTWKENYP KASAEIAGDR KYDVYMGIDV FGRGTYGGGQ WTANVALDLL KSSNVSAAIF
APGWVYETEQ PPDFYTAQNK WWSLVEKSWG IVQTYPQVLP FYSDFNQGLG SHTSLGGRKL
SEAPWYNISC QSLQPFLEFN EGRNSETIQV TVDGREASYN GGGNVSFRGK LKRNAHFTAR
LFKPQLQLSA APISIFFSVK SDKRSELSIL LHFSSPSQEK KSMLMVPNES INRFGDMFLP
CLLTSKQTTS GWTVHETNLV LDGHTLTEIS AFCSRPDDLT EETNTLEYFA LLGHISIKSQ
QKAKVYPLAS SWVIEAHHVK FVPGDSGSKT LSCKLEWRLK HPEEDSVFPK YNVYAENLSS
SEYRPRKVME EPRSEKVFLG TAHVDAYYVS EMVVGSDVKG VRFVVQTCGE DGSWQELDAS
PNLVVEVERV SSKLCCCGLI
