AGAL1_ARATH
ID AGAL1_ARATH Reviewed; 410 AA.
AC Q9FT97; Q8RWB9;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Alpha-galactosidase 1 {ECO:0000303|PubMed:15034167};
DE Short=AtAGAL1 {ECO:0000303|PubMed:15034167};
DE EC=3.2.1.22 {ECO:0000250|UniProtKB:Q9FXT4};
DE AltName: Full=Alpha-D-galactoside galactohydrolase 1 {ECO:0000305};
DE AltName: Full=Melibiase 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=AGAL1 {ECO:0000303|PubMed:15034167};
GN OrderedLocusNames=At5g08380 {ECO:0000312|Araport:AT5G08380};
GN ORFNames=F8L15.110 {ECO:0000312|EMBL:CAC08338.1};
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|Proteomes:UP000006548};
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].
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 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}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR EMBL; AL392174; CAC08338.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91292.1; -; Genomic_DNA.
DR EMBL; AY093200; AAM13199.1; -; mRNA.
DR EMBL; BT008497; AAP37856.1; -; mRNA.
DR RefSeq; NP_196455.1; NM_120922.5.
DR AlphaFoldDB; Q9FT97; -.
DR SMR; Q9FT97; -.
DR STRING; 3702.AT5G08380.1; -.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR MetOSite; Q9FT97; -.
DR PaxDb; Q9FT97; -.
DR PRIDE; Q9FT97; -.
DR ProMEX; Q9FT97; -.
DR ProteomicsDB; 244697; -.
DR EnsemblPlants; AT5G08380.1; AT5G08380.1; AT5G08380.
DR GeneID; 830736; -.
DR Gramene; AT5G08380.1; AT5G08380.1; AT5G08380.
DR KEGG; ath:AT5G08380; -.
DR Araport; AT5G08380; -.
DR TAIR; locus:2150778; AT5G08380.
DR eggNOG; KOG2366; Eukaryota.
DR HOGENOM; CLU_013093_2_2_1; -.
DR InParanoid; Q9FT97; -.
DR OMA; NAFGCDI; -.
DR OrthoDB; 964130at2759; -.
DR PhylomeDB; Q9FT97; -.
DR BioCyc; ARA:AT5G08380-MON; -.
DR PRO; PR:Q9FT97; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FT97; baseline and differential.
DR Genevisible; Q9FT97; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA: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 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 2: Evidence at transcript level;
KW Apoplast; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..410
FT /note="Alpha-galactosidase 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431845"
FT ACT_SITE 175
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT ACT_SITE 230
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT BINDING 96..97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT BINDING 208..212
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06280"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 66..98
FT /evidence="ECO:0000250|UniProtKB:P06280"
FT DISULFID 146..177
FT /evidence="ECO:0000250|UniProtKB:P06280"
FT CONFLICT 78
FT /note="D -> N (in Ref. 3; AAM13199/AAP37856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 45709 MW; F68C52E35FC11F0A CRC64;
MSRRAMVIKM PILMILISSM VMTMVESSRS VNNGHDDSEI LRRHLLTNGL GVTPPMGWNS
WNHFSCNIDE KMIKETADAL VTTGLSKLGY NYVNIDDCWA EISRDSKGSL VPKKSTFPSG
IKAVADYVHS KGLKLGIYSD AGYFTCSKTM PGSLGYEEHD AKTFAEWGID YLKYDNCNSD
GSKPTVRYPV MTRALMKSGR PIFHSLCEWG DMHPALWGSP VGNSWRTTND IKDTWLSMIS
IADMNEVYAE HARPGGWNDP DMLEVGNGGM TKDEYIVHFS IWAISKAPLL LGCDIRNMTK
ETMEIVANKE VIAINQDPHG VQAKKVRMEG DLEVWAGPLS GYRVALLLLN RGPSRTSITA
LWEDIEIPAN SIVEARDLWE HQTLKQKFVG NLTATVDSHA CKLYVLKPVA
