MANA3_ARATH
ID MANA3_ARATH Reviewed; 1047 AA.
AC Q9FKW9;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable alpha-mannosidase At5g66150 {ECO:0000305};
DE EC=3.2.1.24 {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=At5g66150 {ECO:0000312|Araport:AT5G66150};
GN ORFNames=K2A18.23 {ECO:0000312|EMBL:BAB10420.1};
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).
CC -!- FUNCTION: Liberates mannose from p-nitrophenyl-alpha-D-mannoside in
CC vitro. {ECO:0000250|UniProtKB:P94078}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues
CC in alpha-D-mannosides.; EC=3.2.1.24;
CC Evidence={ECO:0000250|UniProtKB:P94078};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q29451};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q29451};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q29451}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250|UniProtKB:P94078}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB011474; BAB10420.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98165.1; -; Genomic_DNA.
DR RefSeq; NP_201416.1; NM_126013.2.
DR AlphaFoldDB; Q9FKW9; -.
DR SMR; Q9FKW9; -.
DR STRING; 3702.AT5G66150.1; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR PaxDb; Q9FKW9; -.
DR PRIDE; Q9FKW9; -.
DR ProteomicsDB; 250820; -.
DR EnsemblPlants; AT5G66150.1; AT5G66150.1; AT5G66150.
DR GeneID; 836747; -.
DR Gramene; AT5G66150.1; AT5G66150.1; AT5G66150.
DR KEGG; ath:AT5G66150; -.
DR Araport; AT5G66150; -.
DR TAIR; locus:2156857; AT5G66150.
DR eggNOG; KOG1959; Eukaryota.
DR HOGENOM; CLU_004690_2_0_1; -.
DR InParanoid; Q9FKW9; -.
DR OrthoDB; 201312at2759; -.
DR PhylomeDB; Q9FKW9; -.
DR BioCyc; ARA:AT5G66150-MON; -.
DR PRO; PR:Q9FKW9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKW9; baseline and differential.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR Gene3D; 1.20.1270.50; -; 2.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR041147; GH38_C.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF17677; Glyco_hydro38C2; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome; Signal; Vacuole; Zinc.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1047
FT /note="Probable alpha-mannosidase At5g66150"
FT /evidence="ECO:0000255"
FT /id="PRO_5006751720"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 857
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 455..465
FT /evidence="ECO:0000250|UniProtKB:C0HJB3"
FT DISULFID 476..484
FT /evidence="ECO:0000250|UniProtKB:C0HJB3"
FT DISULFID 855..860
FT /evidence="ECO:0000250|UniProtKB:C0HJB3"
SQ SEQUENCE 1047 AA; 118008 MW; DAC7CEE58DCBC108 CRC64;
MEKPGMSLLK GSLCVIVFLL LLSLVESVKG GGYVKYGTEA KVVPGKLNVH LVPHSHDDVG
WLKTVDQYYV GSNNRIQNAC VRNVLDSVVD SLLRDPNRKF VFAEMAFFTR WWEEQSPERQ
EQVRRLVKSG QLEFVNGGWA MNDEATCHYI DMIDQTTKGH RFIKQQFNTT PRAAWQIDPF
GHSSVQAYLL GAELGLDSVH FARIDYQDRE KRKAEKSLEV IWRGSKTLDS SSQIFTNIFF
VHYGPPTGFH YEVTDDYVPL QDNPRFDGYN IKEAVNDFVN ASLVYANVSR GNHVMWTMGD
DFQYQFAESW FRQMDRLIHY VNKDGRVNAL YSTPSLYVDA KNVANVTWPL KTHDFFPYAD
RAYAYWTGYF TSRPALKRYV RALSGYYMAA RQLEFLVGKN SGGPNTYSLG DALGIAQHHD
AVTGTAKQHV TNDYMKRLAL GASEAEAVVN SALACLMNKA PKGGCTKPAI AFSQQCSLMN
ISYCPSTEET LPGQKSLILV AYNSLGWNRT EIIRIPVNDA GLSVEDSSGN TLDAQYIPMD
NVTSNLRSFY TKAYLGISSL QRPKYWLVFK AKVPPLGWNT FFISKASAQG SNNHKHSSVM
LSPMNNTTEI GPGNLKMVFS SDSGRLERMY NSRTGADIKV DQNYFWYASN VGDAKDPQVS
GAYIFRPNGS LAYPVSSSKI CTVTSAFIGN GNVQSKLQIV RGPLIDEVHQ QFSPWVAQVV
RLYKEKEHAE FEFTIGPISV GKGHLTGKEI ITRMVTDMTT AKEFYTDSNG RDFLKRVRDN
RTDWHLEVNE PIAGNYYPLN LGMYIKDEKA ELSVLVDRAT GGASIKDGEI ELMLHRRTSM
DDSRGVEESL VETVCVNDTC AGLTIRGNYY VSINKVGEGG RWRRETGQEI YSPLLMAFAH
ENKEKWKASN TVKGYAMDHL YTLPQNIALI TLEELDLGNV LLRLAHLYEA GEDSDYSKIA
KVELKKLFSG KMIKEVTEMS LSANQEKVKM KEKMKWKVEG EAEQPSSPLR GGPVDKSTLV
VELGPMEIRT FVVQFYQKQR RRKLFVG
