ID   PGLR3_MAIZE             Reviewed;         410 AA.
AC   P35339;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=PG2C;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Missouri 17; TISSUE=Leaf;
RX   PubMed=8433375; DOI=10.1006/jmbi.1993.1084;
RA   Barakate A., Martin W., Quigley F., Mache R.;
RT   "Characterization of a multigene family encoding an exopolygalacturonase in
RT   maize.";
RL   J. Mol. Biol. 229:797-801(1993).
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   -!- TISSUE SPECIFICITY: Pollen.
CC   -!- DEVELOPMENTAL STAGE: Late stages of pollen development.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; X66422; CAA47052.1; -; Genomic_DNA.
DR   PIR; S30067; S30067.
DR   AlphaFoldDB; P35339; -.
DR   SMR; P35339; -.
DR   STRING; 4577.GRMZM2G160526_P01; -.
DR   Allergome; 683; Zea m 13.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   PaxDb; P35339; -.
DR   MaizeGDB; 65847; -.
DR   eggNOG; ENOG502QRSR; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P35339; baseline.
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..22
FT   CHAIN           23..410
FT                   /note="Exopolygalacturonase"
FT                   /id="PRO_0000024808"
FT   REPEAT          192..218
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          219..240
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          242..262
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          272..293
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          337..377
FT                   /note="PbH1 5"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        233
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        235..252
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        364..370
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        393..409
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
SQ   SEQUENCE   410 AA;  43297 MW;  5BD1310F588AE7CA CRC64;
     MACIDNAMRA LFLLALFCVV HGEKAKSKDN DAKASGPGGS FDITKLGASG NGKTDSTKAV
     QEAWASACGG TGKQTILIPK GDFLVGPLNF TGPCKGDVTI QVNGNLLATT DLSQYKDHGN
     WIEILRVDNL VITGKGKLDG QGPAVWSKNS CVKKYDCKIL PNSLVMDFVN NGEVSGITLL
     NSKFFHMNMY KCKDMLIKDV NVTAPGDSPN TDGIHMGDSS GVTITNTVIG VGDDCISIGP
     GTSKVNITGV TCGPGHGISI GSLGRYKDEK DVTDINVKDC TLKKTANGVR IKAYEDAASV
     LTASKIHYEN IKMEDSGYPI IIDMKYCPNK LCTANGASKV TVKDVTFKNI TGTSSTPEAV
     NLLCTAKIPC TGVTMDDVNI KYSGTNNKTM AVCKNAKGSA KGCLKELACF