AGAL3_ARATH
ID AGAL3_ARATH Reviewed; 437 AA.
AC Q8VXZ7; F4IZE4; Q9LYL2;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Alpha-galactosidase 3 {ECO:0000303|PubMed:15034167};
DE Short=AtAGAL3 {ECO:0000303|PubMed:15034167};
DE EC=3.2.1.22 {ECO:0000250|UniProtKB:Q9FXT4};
DE AltName: Full=Alpha-D-galactoside galactohydrolase 3 {ECO:0000305};
DE AltName: Full=Melibiase {ECO:0000305};
DE Flags: Precursor;
GN Name=AGAL3 {ECO:0000303|PubMed:15034167};
GN OrderedLocusNames=At3g56310 {ECO:0000312|Araport:AT3G56310};
GN ORFNames=F18O21.270 {ECO:0000312|EMBL:CAB87430.1};
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 {ECO:0000312|EMBL:AAL67017.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP INDUCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12773619; DOI=10.1073/pnas.1230987100;
RA Rojo E., Zouhar J., Carter C., Kovaleva V., Raikhel N.V.;
RT "A unique mechanism for protein processing and degradation in Arabidopsis
RT thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7389-7394(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15034167; DOI=10.1104/pp.103.036210;
RA Tapernoux-Luthi E.M., Bohm A., Keller F.;
RT "Cloning, functional expression, and characterization of the raffinose
RT oligosaccharide chain elongation enzyme, galactan:galactan
RT galactosyltransferase, from common bugle leaves.";
RL Plant Physiol. 134:1377-1387(2004).
CC -!- FUNCTION: May regulate leaf (and possibly other organ) development by
CC functioning in cell wall loosening and cell wall expansion.
CC {ECO:0000250|UniProtKB:Q8RX86}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC residues in alpha-D-galactosides, including galactose
CC oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC Evidence={ECO:0000250|UniProtKB:Q9FXT4};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06280}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:Q8RX86}. Secreted, extracellular space, apoplast
CC {ECO:0000250|UniProtKB:Q8RX86}. Vacuole {ECO:0000305|PubMed:12773619}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VXZ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VXZ7-2; Sequence=VSP_057450;
CC -!- INDUCTION: May be processed or degraded in a VPEgamma-dependent manner
CC in vacuoles. {ECO:0000305|PubMed:12773619}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87430.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL163763; CAB87430.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE79507.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79508.1; -; Genomic_DNA.
DR EMBL; AY074321; AAL67017.1; -; mRNA.
DR EMBL; AY114020; AAM45068.1; -; mRNA.
DR PIR; T47748; T47748.
DR RefSeq; NP_191190.2; NM_115489.6. [Q8VXZ7-1]
DR RefSeq; NP_974447.1; NM_202718.2. [Q8VXZ7-2]
DR AlphaFoldDB; Q8VXZ7; -.
DR SMR; Q8VXZ7; -.
DR STRING; 3702.AT3G56310.1; -.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR PaxDb; Q8VXZ7; -.
DR PRIDE; Q8VXZ7; -.
DR ProteomicsDB; 244880; -. [Q8VXZ7-1]
DR EnsemblPlants; AT3G56310.1; AT3G56310.1; AT3G56310. [Q8VXZ7-1]
DR EnsemblPlants; AT3G56310.2; AT3G56310.2; AT3G56310. [Q8VXZ7-2]
DR GeneID; 824798; -.
DR Gramene; AT3G56310.1; AT3G56310.1; AT3G56310. [Q8VXZ7-1]
DR Gramene; AT3G56310.2; AT3G56310.2; AT3G56310. [Q8VXZ7-2]
DR KEGG; ath:AT3G56310; -.
DR Araport; AT3G56310; -.
DR TAIR; locus:2078416; AT3G56310.
DR eggNOG; KOG2366; Eukaryota.
DR HOGENOM; CLU_013093_2_2_1; -.
DR InParanoid; Q8VXZ7; -.
DR OMA; AMTPTMG; -.
DR OrthoDB; 964130at2759; -.
DR PhylomeDB; Q8VXZ7; -.
DR BioCyc; ARA:AT3G56310-MON; -.
DR PRO; PR:Q8VXZ7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VXZ7; baseline and differential.
DR Genevisible; Q8VXZ7; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0004557; F:alpha-galactosidase activity; IDA:TAIR.
DR GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR CDD; cd14792; GH27; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR041233; Melibiase_C.
DR PANTHER; PTHR11452; PTHR11452; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17801; Melibiase_C; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoplast; Cell wall;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Secreted; Signal; Vacuole.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..437
FT /note="Alpha-galactosidase 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431847"
FT ACT_SITE 193
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT ACT_SITE 248
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT BINDING 115..116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT BINDING 226..230
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 85..117
FT /evidence="ECO:0000250|UniProtKB:P06280"
FT DISULFID 165..195
FT /evidence="ECO:0000250|UniProtKB:P06280"
FT VAR_SEQ 115..138
FT /note="Missing (in isoform 2)"
FT /id="VSP_057450"
SQ SEQUENCE 437 AA; 48363 MW; 5DC7C91065C8B033 CRC64;
MVIMKKMKDS VLFLVVGLFS LSVLVSQSIA GRVKAPLLQS NTGGLVFSKS FNSIYDTSMY
GRLQLNNGLA RTPQMGWNSW NFFACNINET VIKETADALV SSGLADLGYI HVNIDDCWSN
LLRDSEGQLV PHPETFPSGI KLLADYVHSK GLKLGIYSDA GVFTCEVHPG SLFHEVDDAD
IFASWGVDYL KYDNCFNLGI KPIERYPPMR DALNATGRSI FYSLCEWGVD DPALWAKEVG
NSWRTTDDIN DTWASMTTIA DLNNKWAAYA GPGGWNDPDM LEIGNGGMTY EEYRGHFSIW
ALMKAPLLIG CDVRNMTAET LEILSNKEII AVNQDPLGVQ GRKIQANGEN DCQQVWSGPL
SGDRMVVALW NRCSEPATIT ASWDMIGLES TISVSVRDLW QHKDVTENTS GSFEAQVDAH
DCHMYVLTPQ TVSHSDV
