AGAL2_ARATH
ID AGAL2_ARATH Reviewed; 396 AA.
AC Q8RX86; B9DGL8; Q9FT98;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Alpha-galactosidase 2 {ECO:0000303|PubMed:15034167};
DE Short=AtAGAL2 {ECO:0000303|PubMed:15034167};
DE EC=3.2.1.22 {ECO:0000250|UniProtKB:Q9FXT4};
DE AltName: Full=Alpha-D-galactoside galactohydrolase 2 {ECO:0000305};
DE AltName: Full=Melibiase {ECO:0000305};
DE Flags: Precursor;
GN Name=AGAL2 {ECO:0000303|PubMed:15034167};
GN OrderedLocusNames=At5g08370 {ECO:0000312|Araport:AT5G08370};
GN ORFNames=F8L15.100 {ECO:0000312|EMBL:CAC08337.1};
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:AAL90902.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf {ECO:0000312|EMBL:BAH19885.1};
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=16845526; DOI=10.1007/s00425-006-0350-9;
RA Chrost B., Kolukisaoglu U., Schulz B., Krupinska K.;
RT "An alpha-galactosidase with an essential function during leaf
RT development.";
RL Planta 225:311-320(2007).
RN [8]
RP SUBCELLULAR LOCATION, INDUCTION BY VERTICILLIUM LONGISPORUM, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22363647; DOI=10.1371/journal.pone.0031435;
RA Floerl S., Majcherczyk A., Possienke M., Feussner K., Tappe H., Gatz C.,
RA Feussner I., Kues U., Polle A.;
RT "Verticillium longisporum infection affects the leaf apoplastic proteome,
RT metabolome, and cell wall properties in Arabidopsis thaliana.";
RL PLoS ONE 7:E31435-E31435(2012).
CC -!- FUNCTION: May regulate leaf (and possibly other organ) development by
CC functioning in cell wall loosening and cell wall expansion.
CC {ECO:0000269|PubMed:16845526}.
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:0000269|PubMed:16845526}. Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:22363647}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RX86-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RX86-2; Sequence=VSP_057449;
CC -!- INDUCTION: By Verticillium longisporum (VL43), in apoplasm.
CC {ECO:0000269|PubMed:22363647}.
CC -!- DISRUPTION PHENOTYPE: Increased rosette leaves number with a curly
CC surface leaf morphology and delayed flowering.
CC {ECO:0000269|PubMed:16845526}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC08337.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL392174; CAC08337.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91290.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91291.1; -; Genomic_DNA.
DR EMBL; AY090238; AAL90902.1; -; mRNA.
DR EMBL; BT000619; AAN18186.1; -; mRNA.
DR EMBL; AK317201; BAH19885.1; -; mRNA.
DR EMBL; AY085529; AAM62753.1; -; mRNA.
DR RefSeq; NP_001031855.1; NM_001036778.2. [Q8RX86-2]
DR RefSeq; NP_568193.1; NM_120921.5. [Q8RX86-1]
DR AlphaFoldDB; Q8RX86; -.
DR SMR; Q8RX86; -.
DR STRING; 3702.AT5G08370.1; -.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR iPTMnet; Q8RX86; -.
DR PaxDb; Q8RX86; -.
DR PRIDE; Q8RX86; -.
DR ProteomicsDB; 244733; -. [Q8RX86-1]
DR EnsemblPlants; AT5G08370.1; AT5G08370.1; AT5G08370. [Q8RX86-1]
DR EnsemblPlants; AT5G08370.2; AT5G08370.2; AT5G08370. [Q8RX86-2]
DR GeneID; 830735; -.
DR Gramene; AT5G08370.1; AT5G08370.1; AT5G08370. [Q8RX86-1]
DR Gramene; AT5G08370.2; AT5G08370.2; AT5G08370. [Q8RX86-2]
DR KEGG; ath:AT5G08370; -.
DR Araport; AT5G08370; -.
DR TAIR; locus:2150763; AT5G08370.
DR eggNOG; KOG2366; Eukaryota.
DR HOGENOM; CLU_013093_2_2_1; -.
DR InParanoid; Q8RX86; -.
DR OMA; DDLWDRW; -.
DR OrthoDB; 964130at2759; -.
DR PhylomeDB; Q8RX86; -.
DR BioCyc; ARA:AT5G08370-MON; -.
DR PRO; PR:Q8RX86; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RX86; baseline and differential.
DR Genevisible; Q8RX86; AT.
DR GO; GO:0048046; C:apoplast; IDA:UniProtKB.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; 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; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR GO; GO:0009911; P:positive regulation of flower development; IMP:TAIR.
DR GO; GO:0009620; P:response to fungus; IDA:UniProtKB.
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.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..396
FT /note="Alpha-galactosidase 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431846"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT BINDING 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT BINDING 194..198
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 52..84
FT /evidence="ECO:0000250|UniProtKB:P06280"
FT DISULFID 132..163
FT /evidence="ECO:0000250|UniProtKB:P06280"
FT VAR_SEQ 1..27
FT /note="MVLLSFSLRFIAFTLTITLTQIADGFQ -> M (in isoform 2)"
FT /id="VSP_057449"
SQ SEQUENCE 396 AA; 44037 MW; 6859823801D235B6 CRC64;
MVLLSFSLRF IAFTLTITLT QIADGFQSRM LMNNGLALSP QMGWNSWNHF QCNINETLIK
QTADAMVSSG LSAIGYKYIN IDDCWGELKR DSQGSLVAKA STFPSGIKAL SDYVHSKGLK
LGIYSDAGTL TCSQTMPGSL GHEEQDAKTF ASWGIDYLKY DNCENTGTSP RERYPKMSKA
LLNSGRSIFF SLCEWGQEDP ATWAGDIGNS WRTTGDIQDN WKSMTLIADQ NDRWASYARP
GSWNDPDMLE VGNGGMTKEE YMSHFSIWAL AKAPLLIGCD LRSMDKVTFE LLSNKEVIAV
NQDKLGIQGK KVKKEGDLEV WAGPLSKKRV AVILWNRGSA SANITARWAE IGLNSSDIVN
ARDLWEHSTY SCVKKQLSAL VEPHACKMYT LTRRKA
