PGLR_GIBFU
ID PGLR_GIBFU Reviewed; 373 AA.
AC Q07181;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Polygalacturonase;
DE Short=PG;
DE EC=3.2.1.15;
DE AltName: Full=FmPG;
DE AltName: Full=Pectinase;
DE Flags: Precursor;
GN Name=PGA;
OS Gibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium
OS fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=5127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX AGRICOLA=IND93032473;
RA Caprari C., Richter A., Bergmann C., Lo Cicero S., Salvi G., Cervone F.,
RA de Lorenzo G.;
RT "Cloning and characterization of a gene encoding the endopolygalacturonase
RT of Fusarium moniliforme.";
RL Mycol. Res. 97:497-505(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 25-373, AND MUTAGENESIS OF
RP HIS-188; ASP-191; 212-ASP-ASP-213; ARG-267 AND LYS-269.
RX PubMed=11687632; DOI=10.1073/pnas.231473698;
RA Federici L., Caprari C., Mattei B., Savino C., Di Matteo A., De Lorenzo G.,
RA Cervone F., Tsernoglou D.;
RT "Structural requirements of endopolygalacturonase for the interaction with
RT PGIP (polygalacturonase-inhibiting protein).";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13425-13430(2001).
CC -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in
CC the smooth region of the plant cell wall.
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:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; L02239; AAA74586.1; -; Genomic_DNA.
DR PDB; 1HG8; X-ray; 1.73 A; A=25-373.
DR PDBsum; 1HG8; -.
DR AlphaFoldDB; Q07181; -.
DR SMR; Q07181; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR CLAE; PGA28A_GIBMO; -.
DR eggNOG; ENOG502QW1P; Eukaryota.
DR BRENDA; 3.2.1.15; 2425.
DR SABIO-RK; Q07181; -.
DR EvolutionaryTrace; Q07181; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
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; 8.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Repeat; Secreted; Signal; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..373
FT /note="Polygalacturonase"
FT /id="PRO_0000024786"
FT REPEAT 136..158
FT /note="PbH1 1"
FT REPEAT 159..197
FT /note="PbH1 2"
FT REPEAT 198..219
FT /note="PbH1 3"
FT REPEAT 220..240
FT /note="PbH1 4"
FT REPEAT 249..270
FT /note="PbH1 5"
FT REPEAT 278..300
FT /note="PbH1 6"
FT REPEAT 312..333
FT /note="PbH1 7"
FT REPEAT 345..369
FT /note="PbH1 8"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..42
FT DISULFID 214..230
FT DISULFID 340..345
FT DISULFID 364..371
FT MUTAGEN 188
FT /note="H->P: Reduces activity by 98.2%. Lowers affinity for
FT substrate 50-fold."
FT /evidence="ECO:0000269|PubMed:11687632"
FT MUTAGEN 191
FT /note="D->A: Loss of activity. No effect on Km for
FT substrate."
FT /evidence="ECO:0000269|PubMed:11687632"
FT MUTAGEN 212..213
FT /note="DD->EE: Loss of activity. No effect on Km for
FT substrate."
FT /evidence="ECO:0000269|PubMed:11687632"
FT MUTAGEN 212..213
FT /note="DD->NN: Loss of activity. No effect on Km for
FT substrate."
FT /evidence="ECO:0000269|PubMed:11687632"
FT MUTAGEN 267
FT /note="R->A: Loss of activity. Lowers affinity for
FT substrate over 10-fold."
FT /evidence="ECO:0000269|PubMed:11687632"
FT MUTAGEN 269
FT /note="K->E: Reduces activity by 99.87%. Lowers affinity
FT for substrate over 10-fold."
FT /evidence="ECO:0000269|PubMed:11687632"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1HG8"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1HG8"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1HG8"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 127..143
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 160..170
FT /evidence="ECO:0007829|PDB:1HG8"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1HG8"
FT TURN 179..183
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 199..209
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 214..233
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 248..271
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 276..302
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 313..329
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:1HG8"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:1HG8"
SQ SEQUENCE 373 AA; 38915 MW; D77BCACAC7FFBD8F CRC64;
MVRNIVSRLC SQLFALPSSS LQERDPCSVT EYSGLATAVS SCKNIVLNGF QVPTGKQLDL
SSLQNDSTVT FKGTTTFATT ADNDFNPIVI SGSNITITGA SGHVIDGNGQ AYWDGKGSNS
NSNQKPDHFI VVQKTTGNSK ITNLNIQNWP VHCFDITGSS QLTISGLILD NRAGDKPNAK
SGSLPAAHNT DGFDISSSDH VTLDNNHVYN QDDCVAVTSG TNIVVSNMYC SGGHGLSIGS
VGGKSDNVVD GVQFLSSQVV NSQNGCRIKS NSGATGTINN VTYQNIALTN ISTYGVDVQQ
DYLNGGPTGK PTNGVKISNI KFIKVTGTVA SSAQDWFILC GDGSCSGFTF SGNAITGGGK
TSSCNYPTNT CPS
