PGLRX_COCCA
ID PGLRX_COCCA Reviewed; 446 AA.
AC Q00359;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Exopolygalacturonase;
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=PGX1;
OS Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=5017;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90305 / SB111 / 2R15;
RX PubMed=9546185; DOI=10.1128/aem.64.4.1497-1503.1998;
RA Scott-Craig J.S., Cheng Y.Q., Cervone F., de Lorenzo G., Pitkin J.W.,
RA Walton J.D.;
RT "Targeted mutants of Cochliobolus carbonum lacking the two major
RT extracellular polygalacturonases.";
RL Appl. Environ. Microbiol. 64:1497-1503(1998).
CC -!- FUNCTION: Hydrolysis of 1,4-alpha-D-galactosiduronic linkages in
CC pectate and other galacturonans.
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.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; L48982; AAC26146.1; -; Genomic_DNA.
DR AlphaFoldDB; Q00359; -.
DR SMR; Q00359; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR CLAE; PGX28A_COCCA; -.
DR PHI-base; PHI:115; -.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProt.
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; 6.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..446
FT /note="Exopolygalacturonase"
FT /id="PRO_0000024823"
FT REPEAT 236..257
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 259..279
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 290..311
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 332..353
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 367..398
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT REPEAT 403..434
FT /note="PbH1 6"
FT /evidence="ECO:0000255"
FT ACT_SITE 250
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT ACT_SITE 273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 252..269
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 397..403
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 424..436
FT /evidence="ECO:0000250|UniProtKB:O74213"
SQ SEQUENCE 446 AA; 47764 MW; 71C535D5720D6325 CRC64;
MRVTDIISCA LLQASIALST PVEELGAKAV VAKRFPPVPF LPGKASSVPG SRNKTCMLKA
LGGGKDDSAN ILSAVKQCNN GGHVVFPKGQ QFTIGTALDL TFLNGIDLDI QGTIQFTNDT
DYWQANSFKQ VFQNATTFFQ LGGKDINVYG GGTLDGNGQA WYDLYAKDIY ILRPILFGLI
GAKNAKISDL KFRYSPQWYT LVANSSQVVF SNIDIFGDSK SKNPAKNTDG WDTYRSDNII
IQNSNINNGD DCVSFKPNST NILVQNLVCN GSHGISVGSL GQYPGEVDIV ENILVRNISM
SNASDGARIK VWPGASSALS GDLQGGGGSG AVRNVTYDGM IVKNVDYAIE ITQCYGQKNL
TLCNQFPSNL TISDITIKNF KGTTSKKYDP RVGYVVCSSP KVCSDISIEN IDVKSPSGTN
LFTCANAEGI QSQVNCTVEG DKGGHS
