PGLR1_MAIZE
ID PGLR1_MAIZE Reviewed; 410 AA.
AC P26216;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 142.
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=PG1;
GN and
GN Name=PG2;
GN and
GN Name=PG3;
GN and
GN Name=PG6;
GN and
GN Name=PG14;
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 [MRNA], AND PROTEIN SEQUENCE OF 23-37.
RC STRAIN=cv. Missouri 17; TISSUE=Pollen;
RX PubMed=1932692; DOI=10.1007/bf00028732;
RA Niogret M.F., Dubald M., Mandaron P., Mache R.;
RT "Characterization of pollen polygalacturonase encoded by several cDNA
RT clones in maize.";
RL Plant Mol. Biol. 17:1155-1164(1991).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. B73, and cv. Wisconsin 22;
RX PubMed=1391780; DOI=10.1007/bf00014505;
RA Allen R.L., Lonsdale D.M.;
RT "Sequence analysis of three members of the maize polygalacturonase gene
RT family expressed during pollen development.";
RL Plant Mol. Biol. 20:343-345(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-306.
RX PubMed=8106080; DOI=10.1111/j.1365-313x.1993.tb00177.x;
RA Allen R.L., Lonsdale D.M.;
RT "Molecular characterization of one of the maize polygalacturonase gene
RT family members which are expressed during late pollen development.";
RL Plant J. 3:261-271(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X57627; CAA40850.1; -; mRNA.
DR EMBL; X57628; CAA40851.1; -; mRNA.
DR EMBL; X57743; CAA40910.1; -; mRNA.
DR EMBL; X57575; CAA40803.1; -; mRNA.
DR EMBL; X65844; CAA46679.1; -; Genomic_DNA.
DR EMBL; X65845; CAA46680.1; -; Genomic_DNA.
DR EMBL; X62384; CAA44248.1; -; Genomic_DNA.
DR EMBL; X62385; CAA44249.1; -; Genomic_DNA.
DR EMBL; X66692; CAA47234.1; -; Genomic_DNA.
DR PIR; S18570; S18570.
DR PIR; S25824; S25824.
DR PIR; S30064; S30064.
DR RefSeq; NP_001105432.1; NM_001111962.1.
DR RefSeq; XP_008649073.1; XM_008650851.1.
DR RefSeq; XP_008649076.1; XM_008650854.1.
DR AlphaFoldDB; P26216; -.
DR SMR; P26216; -.
DR STRING; 4577.GRMZM2G320175_P01; -.
DR Allergome; 683; Zea m 13.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; P26216; -.
DR PRIDE; P26216; -.
DR EnsemblPlants; Zm00001eb275980_T001; Zm00001eb275980_P001; Zm00001eb275980.
DR EnsemblPlants; Zm00001eb276010_T001; Zm00001eb276010_P001; Zm00001eb276010.
DR EnsemblPlants; Zm00001eb276020_T001; Zm00001eb276020_P001; Zm00001eb276020.
DR EnsemblPlants; Zm00001eb276030_T001; Zm00001eb276030_P001; Zm00001eb276030.
DR EnsemblPlants; Zm00001eb276060_T001; Zm00001eb276060_P001; Zm00001eb276060.
DR EnsemblPlants; Zm00001eb276090_T001; Zm00001eb276090_P001; Zm00001eb276090.
DR EnsemblPlants; Zm00001eb442160_T001; Zm00001eb442160_P001; Zm00001eb442160.
DR GeneID; 103629733; -.
DR GeneID; 542387; -.
DR Gramene; Zm00001eb275980_T001; Zm00001eb275980_P001; Zm00001eb275980.
DR Gramene; Zm00001eb276010_T001; Zm00001eb276010_P001; Zm00001eb276010.
DR Gramene; Zm00001eb276020_T001; Zm00001eb276020_P001; Zm00001eb276020.
DR Gramene; Zm00001eb276030_T001; Zm00001eb276030_P001; Zm00001eb276030.
DR Gramene; Zm00001eb276060_T001; Zm00001eb276060_P001; Zm00001eb276060.
DR Gramene; Zm00001eb276090_T001; Zm00001eb276090_P001; Zm00001eb276090.
DR Gramene; Zm00001eb442160_T001; Zm00001eb442160_P001; Zm00001eb442160.
DR KEGG; zma:103629733; -.
DR KEGG; zma:542387; -.
DR MaizeGDB; 25864; -.
DR eggNOG; ENOG502QRSR; Eukaryota.
DR HOGENOM; CLU_016031_2_2_1; -.
DR OMA; MACTNNA; -.
DR OrthoDB; 1028572at2759; -.
DR Proteomes; UP000007305; Chromosome 6.
DR ExpressionAtlas; P26216; baseline.
DR Genevisible; P26216; ZM.
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 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:1932692"
FT CHAIN 23..410
FT /note="Exopolygalacturonase"
FT /id="PRO_0000024806"
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 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"
FT VARIANT 359
FT /note="A -> V (in PG14)"
SQ SEQUENCE 410 AA; 43444 MW; 0A6E779644D818BA CRC64;
MACTNNAMRA LFLLVLFCIV HGEKEESKGI DAKASGPGGS FDITKLGASG NGKTDSTKAV
QEAWASACGG TGKQTILIPK GDFLVGQLNF TGPCKGDVTI QVDGNLLATT DLSQYKDHGN
WIEILRVDNL VITGKGNLDG QGPAVWSKNS CTKKYDCKIL PNSLVMDFVN NGEVSGVTLL
NSKFFHMNMY RCKDMLIKDV TVTAPGDSPN TDGIHMGDSS GITITNTVIG VGDDCISIGP
GTSKVNITGV TCGPGHGISI GSLGRYKDEK DVTDINVKDC TLKKTMFGVR IKAYEDAASV
LTVSKIHYEN IKMEDSANPI FIDMKYCPNK LCTANGASKV TVKDVTFKNI TGTSSTPEAV
SLLCTAKVPC TGVTMDDVNV EYSGTNNKTM AICTNAKGST KGCLKELACF
