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Polygalacturonase (PG) (EC 3.2.1.15) (Major pollen allergen Cha o 2) (Pectinase) (allergen Cha o 2)

 PGLR2_CHAOB             Reviewed;         514 AA.
Q7M1E7;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
15-DEC-2003, sequence version 1.
10-MAY-2017, entry version 61.
RecName: Full=Polygalacturonase;
Short=PG;
EC=3.2.1.15;
AltName: Full=Major pollen allergen Cha o 2;
AltName: Full=Pectinase;
AltName: Allergen=Cha o 2;
Flags: Precursor;
Chamaecyparis obtusa (Hinoki false-cypress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Pinidae; Cupressales; Cupressaceae; Chamaecyparis.
NCBI_TaxID=13415;
[1]
NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 51-62.
TISSUE=Pollen;
PubMed=10486272; DOI=10.1006/bbrc.1999.1261;
Mori T., Yokoyama M., Komiyama N., Okano M., Kino K.;
"Purification, identification, and cDNA cloning of Cha o 2, the second
major allergen of Japanese cypress pollen.";
Biochem. Biophys. Res. Commun. 263:166-171(1999).
-!- CATALYTIC ACTIVITY: Random hydrolysis of (1->4)-alpha-D-
galactosiduronic linkages in pectate and other galacturonans.
-!- SUBCELLULAR LOCATION: Secreted. Secreted, cell wall.
-!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family.
{ECO:0000305}.
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PIR; JC7100; JC7100.
ProteinModelPortal; Q7M1E7; -.
SMR; Q7M1E7; -.
Allergome; 198; Cha o 2.
Allergome; 3187; Cha o 2.0101.
CAZy; GH28; Glycoside Hydrolase Family 28.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
Gene3D; 2.160.20.10; -; 1.
InterPro; IPR000743; Glyco_hydro_28.
InterPro; IPR006626; PbH1.
InterPro; IPR012334; Pectin_lyas_fold.
InterPro; IPR011050; Pectin_lyase_fold/virulence.
Pfam; PF00295; Glyco_hydro_28; 1.
SMART; SM00710; PbH1; 5.
SUPFAM; SSF51126; SSF51126; 1.
PROSITE; PS00502; POLYGALACTURONASE; 1.
1: Evidence at protein level;
Allergen; Cell wall; Cell wall biogenesis/degradation;
Direct protein sequencing; Fruit ripening; Glycoprotein; Glycosidase;
Hydrolase; Repeat; Secreted; Signal; Zymogen.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 50 {ECO:0000269|PubMed:10486272}.
/FTId=PRO_0000024814.
CHAIN 51 514 Polygalacturonase.
/FTId=PRO_0000024815.
REPEAT 214 240 PbH1 1.
REPEAT 241 262 PbH1 2.
REPEAT 264 284 PbH1 3.
REPEAT 294 315 PbH1 4.
REPEAT 323 344 PbH1 5.
REPEAT 357 384 PbH1 6.
ACT_SITE 255 255 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10052}.
ACT_SITE 278 278 {ECO:0000255|PROSITE-ProRule:PRU10052}.
CARBOHYD 266 266 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 514 AA; 56073 MW; 68B62DEBDD59C1EC CRC64;
MGMKFMAAVA FLALQLIVMA AAEDQSAQIM LDSDIEQYLR SNRSLKKLVH SRHDAATVFN
VEQYGAVGDG KHDSTEAFAT TWNAACKKAS AVLLVPANKK FFVNNLVFRG PCQPHLSFKV
DGTIVAQPDP ARWKNSKIWL QFAQLTDFNL MGTGVIDGQG QQWWAGQCKV VNGRTVCNDR
NRPTAIKIDY SKSVTVKELT LMNSPEFHLV FGECEGVKIQ GLKIKAPRDS PNTDGIDIFA
SKRFHIEKCV IGTGDDCIAI GTGSSNITIK DLICGPGHGI SIGSLGRDNS RAEVSHVHVN
RAKFIDTQNG LRIKTWQGGS GLASYITYEN VEMINSENPI LINQFYCTSA SACQNQRSAV
QIQGVTYKNI HGTSATAAAI QLMCSDSVPC TGIQLSNVSL KLTSGKPASC VDKNARGFYS
GRLIPTCKNL RPGPSPKEFE LQQQPTTVMD ENKGACAKGD STCISLSSSP PNCKNKCKGC
QPCKPKLIIV HPNKPQDYYP QKWVCSCHNK IYNP


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