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Alpha-galactosidase 2 (AtAGAL2) (EC 3.2.1.22) (Alpha-D-galactoside galactohydrolase 2) (Melibiase)

 AGAL2_ARATH             Reviewed;         396 AA.
Q8RX86; B9DGL8; Q9FT98;
04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
20-JUN-2018, entry version 108.
RecName: Full=Alpha-galactosidase 2 {ECO:0000303|PubMed:15034167};
Short=AtAGAL2 {ECO:0000303|PubMed:15034167};
EC=3.2.1.22 {ECO:0000250|UniProtKB:Q9FXT4};
AltName: Full=Alpha-D-galactoside galactohydrolase 2 {ECO:0000305};
AltName: Full=Melibiase {ECO:0000305};
Flags: Precursor;
Name=AGAL2 {ECO:0000303|PubMed:15034167};
OrderedLocusNames=At5g08370 {ECO:0000312|Araport:AT5G08370};
ORFNames=F8L15.100 {ECO:0000312|EMBL:CAC08337.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000312|EMBL:AAL90902.1};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
TISSUE=Rosette leaf {ECO:0000312|EMBL:BAH19885.1};
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15034167; DOI=10.1104/pp.103.036210;
Tapernoux-Luthi E.M., Bohm A., Keller F.;
"Cloning, functional expression, and characterization of the raffinose
oligosaccharide chain elongation enzyme, galactan:galactan
galactosyltransferase, from common bugle leaves.";
Plant Physiol. 134:1377-1387(2004).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
PubMed=16845526; DOI=10.1007/s00425-006-0350-9;
Chrost B., Kolukisaoglu U., Schulz B., Krupinska K.;
"An alpha-galactosidase with an essential function during leaf
development.";
Planta 225:311-320(2007).
[8]
SUBCELLULAR LOCATION, INDUCTION BY VERTICILLIUM LONGISPORUM, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22363647; DOI=10.1371/journal.pone.0031435;
Floerl S., Majcherczyk A., Possienke M., Feussner K., Tappe H.,
Gatz C., Feussner I., Kues U., Polle A.;
"Verticillium longisporum infection affects the leaf apoplastic
proteome, metabolome, and cell wall properties in Arabidopsis
thaliana.";
PLoS ONE 7:E31435-E31435(2012).
-!- FUNCTION: May regulate leaf (and possibly other organ) development
by functioning in cell wall loosening and cell wall expansion.
{ECO:0000269|PubMed:16845526}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing alpha-D-
galactose residues in alpha-D-galactosides, including galactose
oligosaccharides, galactomannans and galactolipids.
{ECO:0000250|UniProtKB:Q9FXT4}.
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06280}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall
{ECO:0000269|PubMed:16845526}. Secreted, extracellular space,
apoplast {ECO:0000269|PubMed:22363647}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8RX86-1; Sequence=Displayed;
Name=2;
IsoId=Q8RX86-2; Sequence=VSP_057449;
Note=No experimental confirmation available.
{ECO:0000312|EMBL:AED91291.1};
-!- INDUCTION: By Verticillium longisporum (VL43), in apoplasm.
{ECO:0000269|PubMed:22363647}.
-!- DISRUPTION PHENOTYPE: Increased rosette leaves number with a curly
surface leaf morphology and delayed flowering.
{ECO:0000269|PubMed:16845526}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAC08337.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AL392174; CAC08337.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED91290.1; -; Genomic_DNA.
EMBL; CP002688; AED91291.1; -; Genomic_DNA.
EMBL; AY090238; AAL90902.1; -; mRNA.
EMBL; BT000619; AAN18186.1; -; mRNA.
EMBL; AK317201; BAH19885.1; -; mRNA.
EMBL; AY085529; AAM62753.1; -; mRNA.
RefSeq; NP_001031855.1; NM_001036778.2. [Q8RX86-2]
RefSeq; NP_568193.1; NM_120921.5. [Q8RX86-1]
UniGene; At.32587; -.
UniGene; At.48997; -.
ProteinModelPortal; Q8RX86; -.
SMR; Q8RX86; -.
STRING; 3702.AT5G08370.1; -.
CAZy; GH27; Glycoside Hydrolase Family 27.
iPTMnet; Q8RX86; -.
PaxDb; Q8RX86; -.
PRIDE; Q8RX86; -.
EnsemblPlants; AT5G08370.1; AT5G08370.1; AT5G08370. [Q8RX86-1]
EnsemblPlants; AT5G08370.2; AT5G08370.2; AT5G08370. [Q8RX86-2]
GeneID; 830735; -.
Gramene; AT5G08370.1; AT5G08370.1; AT5G08370. [Q8RX86-1]
Gramene; AT5G08370.2; AT5G08370.2; AT5G08370. [Q8RX86-2]
KEGG; ath:AT5G08370; -.
Araport; AT5G08370; -.
TAIR; locus:2150763; AT5G08370.
eggNOG; KOG2366; Eukaryota.
eggNOG; ENOG410XPF1; LUCA.
HOGENOM; HOG000161224; -.
KO; K07407; -.
OMA; SQFITRV; -.
OrthoDB; EOG09360A7S; -.
PhylomeDB; Q8RX86; -.
BioCyc; ARA:AT5G08370-MONOMER; -.
Reactome; R-ATH-1660662; Glycosphingolipid metabolism.
Reactome; R-ATH-6798695; Neutrophil degranulation.
PRO; PR:Q8RX86; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q8RX86; baseline and differential.
Genevisible; Q8RX86; AT.
GO; GO:0048046; C:apoplast; IDA:UniProtKB.
GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
GO; GO:0004557; F:alpha-galactosidase activity; IDA:TAIR.
GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
GO; GO:0009911; P:positive regulation of flower development; IMP:TAIR.
GO; GO:0009620; P:response to fungus; IDA:UniProtKB.
CDD; cd14792; GH27; 1.
Gene3D; 2.60.40.1180; -; 1.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR002241; Glyco_hydro_27.
InterPro; IPR000111; Glyco_hydro_27/36_CS.
InterPro; IPR013780; Glyco_hydro_b.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR035373; Melibiase/NAGA_C.
Pfam; PF16499; Melibiase_2; 1.
Pfam; PF17450; Melibiase_2_C; 1.
PRINTS; PR00740; GLHYDRLASE27.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
1: Evidence at protein level;
Alternative splicing; Apoplast; Cell wall;
Cell wall biogenesis/degradation; Complete proteome; Disulfide bond;
Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted;
Signal.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 396 Alpha-galactosidase 2. {ECO:0000255}.
/FTId=PRO_0000431846.
REGION 82 83 Substrate binding.
{ECO:0000250|UniProtKB:P17050}.
REGION 194 198 Substrate binding. {ECO:0000250}.
ACT_SITE 161 161 Nucleophile.
{ECO:0000250|UniProtKB:P17050}.
ACT_SITE 216 216 Proton donor.
{ECO:0000250|UniProtKB:P17050}.
BINDING 159 159 Substrate.
{ECO:0000250|UniProtKB:P17050}.
BINDING 212 212 Substrate.
{ECO:0000250|UniProtKB:P17050}.
BINDING 216 216 Substrate.
{ECO:0000250|UniProtKB:P17050}.
CARBOHYD 55 55 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 343 343 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 354 354 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 52 84 {ECO:0000250|UniProtKB:P06280}.
DISULFID 132 163 {ECO:0000250|UniProtKB:P06280}.
VAR_SEQ 1 27 MVLLSFSLRFIAFTLTITLTQIADGFQ -> M (in
isoform 2).
/FTId=VSP_057449.
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


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