PGLRX_ASPTU
ID PGLRX_ASPTU Reviewed; 435 AA.
AC Q00293;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Exopolygalacturonase X;
DE Short=ExoPG;
DE EC=3.2.1.67;
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase;
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase;
DE Flags: Precursor;
GN Name=pgaX;
OS Aspergillus tubingensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=5068;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-41; 172-191 AND
RP 301-315, GLYCOSYLATION, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8856078; DOI=10.1111/j.1432-1033.1996.0738h.x;
RA Kester H.C.M., Kusters-Van Someren M.A., Mueller Y., Visser J.;
RT "Primary structure and characterization of an exopolygalacturonase from
RT Aspergillus tubingensis.";
RL Eur. J. Biochem. 240:738-746(1996).
CC -!- FUNCTION: Specific in hydrolyzing the terminal glycosidic bond of
CC polygalacturonic acid and oligogalacturonates.
CC {ECO:0000269|PubMed:8856078}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.2. {ECO:0000269|PubMed:8856078};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; X99795; CAA68128.1; -; Genomic_DNA.
DR PIR; S74208; S74208.
DR AlphaFoldDB; Q00293; -.
DR SMR; Q00293; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR CLAE; PGX28X_ASPTU; -.
DR VEuPathDB; FungiDB:ASPTUDRAFT_856206; -.
DR OMA; YSPQWYT; -.
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; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:8856078"
FT CHAIN 23..435
FT /note="Exopolygalacturonase X"
FT /id="PRO_0000024822"
FT REPEAT 199..229
FT /note="PbH1 1"
FT REPEAT 230..251
FT /note="PbH1 2"
FT REPEAT 253..273
FT /note="PbH1 3"
FT REPEAT 326..347
FT /note="PbH1 4"
FT REPEAT 361..409
FT /note="PbH1 5"
FT REGION 32..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 244
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 246..263
FT /evidence="ECO:0000250"
FT DISULFID 391..397
FT /evidence="ECO:0000250"
FT CONFLICT 25
FT /note="R -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="C -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="P -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 47296 MW; C47CD97FCD1657C0 CRC64;
MRLTHVLSHT LGLLALGATA EAFSRSREAA CGPKKPFRPL PTSQSRDKTC HVRSHGDGTD
DSDYILSALN QCNHGGKVVF DEDKEYIIGT ALNMTFLKNI DLEVLGTILF TNDTDYWQAN
SFKQGFQNAT TFFQLGGEDV NMYGGGTING NGQVWYDLYA EDDLILRPIL MGIIGLNGGT
IGPLKLRYSP QYYHFVANSS NVLFDGIDIS GYSKSDNEAK NTDGWDTYRS NNIVIQNSVI
NNGDDCVSFK PNSTNILVQN LHCNGSHGIS VGSLGQYKDE VDIVENVYVY NISMFNASDM
ARIKVWPGTP SALSADLQGG GGSGSVKNIT YDTALIDNVD WAIEITQCYG QKNTTLCNEY
PSSLTISDVH IKNFRGTTSG SEDPYVGTIV CSSPDTCSDI YTSNINVTSP DGTNDFVCDN
VDESLLSVNC TATSD
