ID   SALK6_KALTU             Reviewed;         401 AA.
AC   W8P8Q3; A0A1X9YLN9;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2017, sequence version 3.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Probable galacturan 1,4-alpha-galacturonidase SALK6 {ECO:0000305};
DE            EC=3.2.1.67 {ECO:0000305};
DE   AltName: Full=Exopolygalacturonase SALK6 {ECO:0000305};
DE   AltName: Full=Pollen allergen Sal k 6 {ECO:0000303|PubMed:28502749};
DE   AltName: Allergen=Sal k 6 {ECO:0000303|PubMed:28502749};
DE   Flags: Precursor;
OS   Kali turgidum (Prickly saltwort) (Salsola kali).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Salsoloideae; Salsoleae; Kali.
OX   NCBI_TaxID=151250;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   ALLERGEN.
RC   TISSUE=Pollen;
RX   PubMed=28502749; DOI=10.1016/j.bbapap.2017.05.007;
RA   Mas S., Oeo-Santos C., Cuesta-Herranz J., Diaz-Perales A., Colas C.,
RA   Fernandez J., Barber D., Rodriguez R., de Los Rios V., Barderas R.,
RA   Villalba M.;
RT   "A relevant IgE-reactive 28kDa protein identified from Salsola kali pollen
RT   extract by proteomics is a natural degradation product of an integral 47kDa
RT   polygalaturonase.";
RL   Biochim. Biophys. Acta 1865:1067-1076(2017).
CC   -!- FUNCTION: May function in depolymerizing pectin during pollen
CC       development, germination, and tube growth. Acts as an exo-
CC       polygalacturonase. {ECO:0000305}.
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         Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Secreted. Secreted, cell wall {ECO:0000305}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE. Induces
CC       basophil activation from blood of S.kali pollen-sensitized patients.
CC       {ECO:0000269|PubMed:28502749}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; KC920919; AHL24657.2; -; mRNA.
DR   EMBL; KY883988; ARS33724.1; -; mRNA.
DR   AlphaFoldDB; W8P8Q3; -.
DR   SMR; W8P8Q3; -.
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   Allergen; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..401
FT                   /note="Probable galacturan 1,4-alpha-galacturonidase SALK6"
FT                   /id="PRO_0000441331"
FT   ACT_SITE        219
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   ACT_SITE        242
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        221..238
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        349..355
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        376..392
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
SQ   SEQUENCE   401 AA;  42066 MW;  8165F64D6E81F93A CRC64;
     MKTFNLPLLV ALFYLFVSVA RSQGPIDITK FGAKPNADAT SALLAAWKEA CAAAAPAKIV
     VPAGEFLLNA VKLQGPCKAP LTIEIAGNFK APADVAQMKG EDTWVKIENV QGLTITCLPT
     GGTFDGQGQA AWKQNKCAQS GMCNSLPYNF RFNTLTNAQI SGIKSLNSKL YHMGVMGCKN
     ITLTGLTIDA PKDSLNTDGM HIGRSNGVHA TNSKIGTGDD CISMGDGAVD VHVEGITCGP
     GHGISIGSMG KFANEAPNTG IFVKNCSFTD TDNGVRIKSW MNSFEASASD LHFEDITVTN
     VLNPVIIDQE YCPYNHCKEK TPSKVKLSKI SFKNVHGAAK SAEVVKLLCS SAVPCDGVEL
     ADIDLTFPGG AAVSQCKNVK PIVTGKQNPV ACGAPATPAA P