PGLR2_ARATH
ID PGLR2_ARATH Reviewed; 444 AA.
AC P49063; Q9SFC9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Exopolygalacturonase clone GBGA483;
DE Short=ExoPG;
DE EC=3.2.1.67;
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase;
DE AltName: Full=Pectinase;
DE Flags: Precursor;
GN OrderedLocusNames=At3g07850; ORFNames=F17A17.19;
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 [MRNA].
RC STRAIN=cv. C24; TISSUE=Flower bud;
RX PubMed=10485285; DOI=10.1007/s004380051042;
RA Torki M., Mandaron P., Thomas F., Quigley F., Mache R., Falconet D.;
RT "Differential expression of a polygalacturonase gene family in Arabidopsis
RT thaliana.";
RL Mol. Gen. Genet. 261:948-952(1999).
RN [2]
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 [3]
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 [4]
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).
CC -!- FUNCTION: May function in depolymerizing pectin during pollen
CC development, germination, and tube growth. Acts as an exo-
CC polygalacturonase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-
CC galacturonosyl](n-1) + alpha-D-galacturonate; Xref=Rhea:RHEA:14117,
CC Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14572, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58658, ChEBI:CHEBI:140523; EC=3.2.1.67;
CC -!- SUBCELLULAR LOCATION: Secreted. Secreted, cell wall.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; X72292; CAA51033.1; -; mRNA.
DR EMBL; AC013483; AAF21195.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74611.1; -; Genomic_DNA.
DR EMBL; AY056173; AAL07022.1; -; mRNA.
DR EMBL; AY091200; AAM14139.1; -; mRNA.
DR PIR; S34200; S34200.
DR RefSeq; NP_187442.1; NM_111664.3.
DR AlphaFoldDB; P49063; -.
DR SMR; P49063; -.
DR STRING; 3702.AT3G07850.1; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR iPTMnet; P49063; -.
DR PaxDb; P49063; -.
DR PRIDE; P49063; -.
DR ProteomicsDB; 235103; -.
DR EnsemblPlants; AT3G07850.1; AT3G07850.1; AT3G07850.
DR GeneID; 819976; -.
DR Gramene; AT3G07850.1; AT3G07850.1; AT3G07850.
DR KEGG; ath:AT3G07850; -.
DR Araport; AT3G07850; -.
DR TAIR; locus:2077442; AT3G07850.
DR eggNOG; ENOG502QTAW; Eukaryota.
DR HOGENOM; CLU_016031_2_2_1; -.
DR InParanoid; P49063; -.
DR OrthoDB; 1028572at2759; -.
DR PhylomeDB; P49063; -.
DR BioCyc; ARA:AT3G07850-MON; -.
DR PRO; PR:P49063; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P49063; baseline and differential.
DR Genevisible; P49063; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 2: Evidence at transcript level;
KW Cell wall; Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..444
FT /note="Exopolygalacturonase clone GBGA483"
FT /id="PRO_0000024800"
FT REPEAT 220..246
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 247..268
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 270..290
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 300..321
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 330..351
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT ACT_SITE 261
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT ACT_SITE 284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 263..280
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 391..397
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 420..436
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT CONFLICT 81
FT /note="S -> G (in Ref. 1; CAA51033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 45600 MW; DF1D4C30FB1C3F11 CRC64;
MVGSHKASGV LLVLLVVMAT TIANGTPVVD KAKNAATAVE DTAKNAATAV GGAAASVGAK
VSGAKPGAAV DVKASGAKGD SKTDDSAAFA AAWKEACAAG STITVPKGEY MVESLEFKGP
CKGPVTLELN GNFKAPATVK TTKPHAGWID FENIADFTLN GNKAIFDGQG SLAWKANDCA
KTGKCNSLPI NIRFTGLTNS KINSITSTNS KLFHMNILNC KNITLSDIGI DAPPESLNTD
GIHIGRSNGV NLIGAKIKTG DDCVSIGDGT ENLIVENVEC GPGHGISIGS LGRYPNEQPV
KGVTVRKCLI KNTDNGVRIK TWPGSPPGIA SNILFEDITM DNVSLPVLID QEYCPYGHCK
AGVPSQVKLS DVTIKGIKGT SATKVAVKLM CSKGVPCTNI ALSDINLVHN GKEGPAVSAC
SNIKPILSGK LVPAACTEVA KPGP
