ID   PGLR1_ARATH             Reviewed;         422 AA.
AC   P49062;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 172.
DE   RecName: Full=Exopolygalacturonase;
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   Name=PGA3; OrderedLocusNames=At1g02790; ORFNames=F22D16.22, T14P4_2;
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 [GENOMIC DNA].
RA   Torki M., Thomas F., Mache R., Mandaron P., Falconet D.;
RT   "Organisation and expression of a family of polygalacturonase gene in
RT   Arabidopsis thaliana.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [4]
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   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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 = alpha-D-
CC         galacturonate + [(1->4)-alpha-D-galacturonosyl](n-1);
CC         Xref=Rhea:RHEA:14117, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14572,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:58658, ChEBI:CHEBI:140523;
CC         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; X72291; CAA51032.1; -; mRNA.
DR   EMBL; Y16230; CAA76127.1; -; Genomic_DNA.
DR   EMBL; AC009525; AAF02888.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27470.1; -; Genomic_DNA.
DR   EMBL; OZ408683; CAO7025820.1; -; Genomic_DNA.
DR   EMBL; AF428425; AAL16194.1; -; mRNA.
DR   EMBL; AY065210; AAL38686.1; -; mRNA.
DR   EMBL; AY133812; AAM91746.1; -; mRNA.
DR   PIR; S34199; S34199.
DR   AlphaFoldDB; P49062; -.
DR   SMR; P49062; -.
DR   FunCoup; P49062; 137.
DR   STRING; 3702.P49062; -.
DR   GlyCosmos; P49062; 3 sites, No reported glycans.
DR   GlyGen; P49062; 3 sites.
DR   PaxDb; 3702-P49062; -.
DR   ProteomicsDB; 236142; -.
DR   KEGG; ath:AT1G02790; -.
DR   Araport; AT1G02790; -.
DR   TAIR; AT1G02790; PGA4.
DR   eggNOG; ENOG502QV2R; Eukaryota.
DR   HOGENOM; CLU_016031_2_2_1; -.
DR   InParanoid; P49062; -.
DR   OMA; FLNTWIQ; -.
DR   OrthoDB; 187139at2759; -.
DR   PhylomeDB; P49062; -.
DR   BioCyc; ARA:AT1G02790-MONOMER; -.
DR   PRO; PR:P49062; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P49062; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; ISM:TAIR.
DR   GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004650; F:polygalacturonase activity; ISS:TAIR.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   FunFam; 2.160.20.10:FF:000096; Exopolygalacturonase clone GBGE184; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 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   PANTHER; PTHR31375; -; 1.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   SMART; SM00710; PbH1; 5.
DR   SUPFAM; SSF51126; Pectin lyase-like; 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..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..422
FT                   /note="Exopolygalacturonase"
FT                   /id="PRO_0000024799"
FT   REPEAT          200..226
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          227..248
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          250..270
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          280..301
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          310..331
FT                   /note="PbH1 5"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        241
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        243..260
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        366..372
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        404..420
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
SQ   SEQUENCE   422 AA;  44430 MW;  17B02E2CE979B46A CRC64;
     MANARSLVAK ANNINVGSLI LMALVFGSCV ANGEYLGGRR GLAANSGNPT VYDITKFGAV
     GDGSTNTFKA FLNTWIQVCD SPVPATLLVP KGTFLAGPVI FAGPCKSKVT VNVIGTIIAT
     TSGYATPEWF LFERVDNLVL TGTGTFHGKG EAVWKADGCG KKVQCNLPPT SLKFRNMKNV
     EINGISSVNA KAFHMFLVKT ENVNIQNIKL TAPAESPNTD GIHLSNADNV SILDSTIATG
     DDCVSVGRGS NNVTVERVIC GPGHGLSVGS LGKYKNEEDV SGIHVNNCTM IETDNGLRIK
     TWGGSDPSKA VDIKFENIIM QSVKNPIIID QNYGSRGGDS QVAISDILFK NIRGTTITKD
     VVQIMCSKSV PCQGVNVVDV NLDYVGKTGG EKKSSSGGLV GALCDNANVI FGGKLSFPMC
     PK
//