ID   PGLR_MEDSA              Reviewed;         421 AA.
AC   Q40312;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Polygalacturonase;
DE            Short=PG;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase;
DE   Flags: Precursor;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. C2-4; TISSUE=Pollen;
RA   Qiu X., Erickson L.;
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May function in the depolymerization of the pectin in its
CC       walls during pollen tube elongation, or in that of the pistil during
CC       pollination. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-
CC         galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Secreted, cell wall
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Pollen specific.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; U20431; AAA62286.1; -; mRNA.
DR   PIR; T09398; T09398.
DR   AlphaFoldDB; Q40312; -.
DR   SMR; Q40312; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004650; F:polygalacturonase 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   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; 4.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   PROSITE; PS00502; POLYGALACTURONASE; 1.
PE   2: Evidence at transcript level;
KW   Cell wall; Cell wall biogenesis/degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Repeat; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..421
FT                   /note="Polygalacturonase"
FT                   /id="PRO_0000024810"
FT   REPEAT          178..204
FT                   /note="PbH1 1"
FT   REPEAT          205..226
FT                   /note="PbH1 2"
FT   REPEAT          258..279
FT                   /note="PbH1 3"
FT   REPEAT          289..310
FT                   /note="PbH1 4"
FT   REGION          394..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        219
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        242
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   421 AA;  43953 MW;  6E1599E2BD9C73DE CRC64;
     MKFSTAIIVS FLFIADFCAA QSGVLDISKF GGKPNSDIGQ ALTSAWNEAC ASTTAAKIVI
     PAGTYQLNGI ELKGPCKAPI ELQVDGTIQA PADPSVIKGT EQWFKFLYMD HLTLSGKGVF
     DGQGATVYKK AAPASAWSGK NSNSKVFMNF GFNFVNNSIV RGVTSKDSKN FHVMVFGCKN
     ITFDGFTITA PGDSPNTDGI HMGKSTDVKI LNTNIGTGDD CVSIGDGSKQ ITVQGVNCGP
     GHGLSVGSLG KFTTEENVEG ITVKNCTLTA TDNGVRIKTW PDAPGTITVS DIHFEDITMT
     NVKNPVIIDQ EYYPWNQCSK KNPSKIKLSK ISFKNVKGTS GTAEGVVLIC SSAVPCDGVE
     LNNVDLKFNG APTTAKCTNV KPLVTGTAPV CQAPGAPAAS TTATPAASKT ATPAAGKSPA
     K